Dickmanns, Achim

[["dc.bibliographiccitation.firstpage","541"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","552"],["dc.bibliographiccitation.volume","121"],["dc.contributor.author","Dierks, T."],["dc.contributor.author","Dickmanns, A."],["dc.contributor.author","Preusser-Kunze, A."],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Mariappan, M."],["dc.contributor.author","Von Figura, K."],["dc.contributor.author","Ficner, R."],["dc.contributor.author","Rudolph, M."],["dc.date.accessioned","2017-09-07T11:54:25Z"],["dc.date.available","2017-09-07T11:54:25Z"],["dc.date.issued","2005"],["dc.description.abstract","Sulfatases are enzymes essential for degradation and remodeling of sulfate esters. Formylglycine (FGly), the key catalytic residue in the active site, is unique to sulfatases. In higher eukaryotes, FGly is generated from a cysteine precursor by the FGly-generating enzyme (FGE). Inactivity of FGE results in multiple sulfatase deficiency (MSD), a fatal autosomal recessive syndrome. Based on the crystal structure, we report that FGE is a single-domain monomer with a surprising paucity of secondary structure and adopts a unique fold. The effect of all 18 missense mutations found in MSD patients is explained by the FGE structure, providing a molecular basis of MSD. The catalytic mechanism of FGly generation was elucidated by six high-resolution structures of FGE in different redox environments. The structures allow formulation of a novel oxygenase mechanism whereby FGE utilizes molecular oxygen to generate FGly via a cysteine sulfenic acid intermediate."],["dc.identifier.doi","10.1016/j.cell.2005.03.001"],["dc.identifier.gro","3143846"],["dc.identifier.isi","000229331200011"],["dc.identifier.pmid","15907468"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3452"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1405"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0092-8674"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5581"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","5593"],["dc.bibliographiccitation.volume","38"],["dc.contributor.author","Kuehn-Hoelsken, Eva"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Hsiao, He-Hsuan"],["dc.contributor.author","Richter, Florian M."],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Urlaub, Henning"],["dc.date.accessioned","2017-09-07T11:45:20Z"],["dc.date.available","2017-09-07T11:45:20Z"],["dc.date.issued","2010"],["dc.description.abstract","Mass spectrometry allows the elucidation of molecular details of the interaction domains of the individual components in macromolecular complexes subsequent to cross-linking of the individual components. Here, we applied chemical and UV cross-linking combined with tandem mass-spectrometric analysis to identify contact sites of the nuclear import adaptor snurportin 1 to the small ribonucleoprotein particle U1 snRNP in addition to the known interaction of m(3)G cap and snurportin 1. We were able to define previously unknown sites of protein-protein and protein-RNA interactions on the molecular level within U1 snRNP. We show that snurportin 1 interacts with its central m(3)G-cap-binding domain with Sm proteins and with its extreme C-terminus with stem-loop III of U1 snRNA. The crosslinking data support the idea of a larger interaction area between snurportin 1 and U snRNPs and the contact sites identified prove useful for modeling the spatial arrangement of snurportin 1 domains when bound to U1 snRNP. Moreover, this suggests a functional nuclear import complex that assembles around the m(3)G cap and the Sm proteins only when the Sm proteins are bound and arranged in the proper orientation to the cognate Sm site in U snRNA."],["dc.identifier.doi","10.1093/nar/gkq272"],["dc.identifier.gro","3142869"],["dc.identifier.isi","000281720500034"],["dc.identifier.pmid","20421206"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7257"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/320"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","0305-1048"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Mapping the binding site of snurportin 1 on native U1 snRNP by cross-linking and mass spectrometry"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4179"],["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","FEBS Journal"],["dc.bibliographiccitation.lastpage","4194"],["dc.bibliographiccitation.volume","281"],["dc.contributor.author","Monecke, Thomas"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2017-09-07T11:45:33Z"],["dc.date.available","2017-09-07T11:45:33Z"],["dc.date.issued","2014"],["dc.description.abstract","Nucleocytoplasmic trafficking in eukaryotic cells is a highly regulated and coordinated process which involves an increasing variety of soluble nuclear transport receptors. Generally, transport receptors specifically bind their cargo and facilitate its transition through nuclear pore complexes, aqueous channels connecting the two compartments. Directionality of such transport events by receptors of the importin beta superfamily requires the interaction with the small GTPase Ras-related nuclear antigen (Ran). While importins need RanGTP to release their cargo in the nucleus and thus to terminate import, exportins recruit cargo in the RanGTP-bound state. The exportin chromosome region maintenance 1 (CRM1) is a highly versatile transport receptor that exports a plethora of different protein and RNP cargoes. Moreover, binding of RanGTP and of cargo to CRM1 are highly cooperative events despite the fact that cargo and RanGTP do not interact directly in crystal structures of assembled export complexes. Integrative approaches have recently unraveled the individual steps of the CRM1 transport cycle at a structural level and explained how the HEAT-repeat architecture of CRM1 provides a framework for the key elements to mediate allosteric interactions with RanGTP, Ran binding proteins and cargo. Moreover, during the last decade, CRM1 has become a more and more appreciated target for anti-cancer drugs. Hence, detailed understanding of the flexibility, the regulatory features and the positive binding cooperativity between CRM1, Ran and cargo is a prerequisite for the development of highly effective drugs. Here we review recent structural advances in the characterization of CRM1 and CRM1-containing complexes with a special emphasis on X-ray crystallographic studies."],["dc.identifier.doi","10.1111/febs.12842"],["dc.identifier.gro","3142060"],["dc.identifier.isi","000342584200016"],["dc.identifier.pmid","24823279"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12823"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4100"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [Sonderforschungsbereich SFB860]"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-blackwell"],["dc.relation.eissn","1742-4658"],["dc.relation.issn","1742-464X"],["dc.rights","CC BY-NC-ND 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/3.0"],["dc.title","Allosteric control of the exportin CRM1 unraveled by crystal structure analysis"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1001750"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","PLoS Biology"],["dc.bibliographiccitation.lastpage","15"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Ahmed, Yasar Luqman"],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Park, Hee-Soo"],["dc.contributor.author","Bayram, Ozgür"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Ni, Min"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Kim, Sun Chang"],["dc.contributor.author","Yu, Jae-Hyuk"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2017-09-07T11:47:00Z"],["dc.date.available","2017-09-07T11:47:00Z"],["dc.date.issued","2013"],["dc.description.abstract","Morphological development of fungi and their combined production of secondary metabolites are both acting in defence and protection. These processes are mainly coordinated by velvet regulators, which contain a yet functionally and structurally uncharacterized velvet domain. Here we demonstrate that the velvet domain of VosA is a novel DNA-binding motif that specifically recognizes an 11-nucleotide consensus sequence consisting of two motifs in the promoters of key developmental regulatory genes. The crystal structure analysis of the VosA velvet domain revealed an unforeseen structural similarity with the Rel homology domain (RHD) of the mammalian transcription factor NF-B. Based on this structural similarity several conserved amino acid residues present in all velvet domains have been identified and shown to be essential for the DNA binding ability of VosA. The velvet domain is also involved in dimer formation as seen in the solved crystal structures of the VosA homodimer and the VosA-VelB heterodimer. These findings suggest that defence mechanisms of both fungi and animals might be governed by structurally related DNA-binding transcription factors."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2013"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2014"],["dc.identifier.doi","10.1371/journal.pbio.1001750"],["dc.identifier.gro","3142241"],["dc.identifier.isi","000329367200028"],["dc.identifier.pmid","24391470"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9579"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6098"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1545-7885"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","The Velvet Family of Fungal Regulators Contains a DNA-Binding Domain Structurally Similar to NF-κB"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","110879"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.volume","39"],["dc.contributor.author","Giansanti, Celeste"],["dc.contributor.author","Manzini, Valentina"],["dc.contributor.author","Dickmanns, Antje"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Palumbieri, Maria Dilia"],["dc.contributor.author","Sanchi, Andrea"],["dc.contributor.author","Kienle, Simon Maria"],["dc.contributor.author","Rieth, Sonja"],["dc.contributor.author","Scheffner, Martin"],["dc.contributor.author","Lopes, Massimo"],["dc.contributor.author","Dobbelstein, Matthias"],["dc.date.accessioned","2022-07-01T07:35:41Z"],["dc.date.available","2022-07-01T07:35:41Z"],["dc.date.issued","2022"],["dc.description.abstract","The MDM2 oncoprotein antagonizes the tumor suppressor p53 by physical interaction and ubiquitination.\r\nHowever, it also sustains the progression of DNA replication forks, even in the absence of functional p53.\r\nHere, we show that MDM2 binds, inhibits, ubiquitinates, and destabilizes poly(ADP-ribose) polymerase 1\r\n(PARP1). When cellular MDM2 levels are increased, this leads to accelerated progression of DNA replication\r\nforks, much like pharmacological inhibition of PARP1. Conversely, overexpressed PARP1 restores normal\r\nfork progression despite elevated MDM2. Strikingly, MDM2 profoundly reduces the frequency of fork\r\nreversal, revealed as four-way junctions through electron microscopy. Depletion of RECQ1 or the primase/\r\npolymerase (PRIMPOL) reverses the MDM2-mediated acceleration of the nascent DNA elongation rate.\r\nMDM2 also increases the occurrence of micronuclei, and it exacerbates camptothecin-induced cell death.\r\nIn conclusion, high MDM2 levels phenocopy PARP inhibition in modulation of fork restart, representing a\r\npotential vulnerability of cancer cells."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2022"],["dc.identifier.doi","10.1016/j.celrep.2022.110879"],["dc.identifier.pii","S2211124722006544"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112236"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-581"],["dc.relation.issn","2211-1247"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://www.elsevier.com/tdm/userlicense/1.0/"],["dc.title","MDM2 binds and ubiquitinates PARP1 to enhance DNA replication fork progression"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","690"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","702"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Port, Sarah A."],["dc.contributor.author","Monecke, Thomas"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Spillner, Christiane"],["dc.contributor.author","Hofele, Romina"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Kehlenbach, Ralph H."],["dc.date.accessioned","2017-09-07T11:43:28Z"],["dc.date.available","2017-09-07T11:43:28Z"],["dc.date.issued","2015"],["dc.description.abstract","CRM1 is the major nuclear export receptor. During translocation through the nuclear pore, transport complexes transiently interact with phenylalanine-glycine (FG) repeats of multiple nucleoporins. On the cytoplasmic side of the nuclear pore, CRM1 tightly interacts with the nucleoporin Nup214. Here, we present the crystal structure of a 117-amino-acid FG-repeat-containing fragment of Nup214, in complex with CRM1, Snurportin 1, and RanGTP at 2.85 angstrom resolution. The structure reveals eight binding sites for Nup214 FG motifs on CRM1, with intervening stretches that are loosely attached to the transport receptor. Nup214 binds to N- and C-terminal regions of CRM1, thereby clamping CRM1 in a closed conformation and stabilizing the export complex. The role of conserved hydrophobic pockets for the recognition of FG motifs was analyzed in biochemical and cell-based assays. Comparative studies with RanBP3 and Nup62 shed light on specificities of CRM1-nucleoporin binding, which serves as a paradigm for transport receptor-nucleoporin interactions."],["dc.description.sponsorship","Open-Access Publikationsfonds 2015"],["dc.identifier.doi","10.1016/j.celrep.2015.09.042"],["dc.identifier.gro","3141804"],["dc.identifier.isi","000363780900006"],["dc.identifier.pmid","26489467"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12544"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1257"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Cell Press"],["dc.relation.issn","2211-1247"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Structural and Functional Characterization of CRM1-Nup214 Interactions Reveals Multiple FG-Binding Sites Involved in Nuclear Export"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","56"],["dc.bibliographiccitation.journal","BMC Structural Biology"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Lakomek, Kristina"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Kettwig, Matthias"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Luebke, Torben"],["dc.date.accessioned","2017-09-07T11:46:52Z"],["dc.date.available","2017-09-07T11:46:52Z"],["dc.date.issued","2009"],["dc.description.abstract","Background: The lysosomal 66.3 kDa protein from mouse is a soluble, mannose 6-phosphate containing protein of so far unknown function. It is synthesized as a glycosylated 75 kDa precursor that undergoes limited proteolysis leading to a 28 kDa N- and a 40 kDa C-terminal fragment. Results: In order to gain insight into the function and the post-translational maturation process of the glycosylated 66.3 kDa protein, three crystal structures were determined that represent different maturation states. These structures demonstrate that the 28 kDa and 40 kDa fragment which have been derived by a proteolytic cleavage remain associated. Mass spectrometric analysis confirmed the subsequent trimming of the C-terminus of the 28 kDa fragment making a large pocket accessible, at the bottom of which the putative active site is located. The crystal structures reveal a significant similarity of the 66.3 kDa protein to several bacterial hydrolases. The core alpha beta beta alpha sandwich fold and a cysteine residue at the N- terminus of the 40 kDa fragment (C249) classify the 66.3 kDa protein as a member of the structurally defined N- terminal nucleophile (Ntn) hydrolase superfamily. Conclusion: Due to the close resemblance of the 66.3 kDa protein to members of the Ntn hydrolase superfamily a hydrolytic activity on substrates containing a non-peptide amide bond seems reasonable. The structural homology which comprises both the overall fold and essential active site residues also implies an autocatalytic maturation process of the lysosomal 66.3 kDa protein. Upon the proteolytic cleavage between S248 and C249, a deep pocket becomes solvent accessible, which harbors the putative active site of the 66.3 kDa protein."],["dc.identifier.doi","10.1186/1472-6807-9-56"],["dc.identifier.gro","3143072"],["dc.identifier.isi","000269745600001"],["dc.identifier.pmid","19706171"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/5749"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/545"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Biomed Central Ltd"],["dc.relation.issn","1471-2237"],["dc.rights","CC BY 2.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.0"],["dc.title","Initial insight into the function of the lysosomal 66.3 kDa protein from mouse by means of X-ray crystallography"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1007845"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","PLOS Genetics"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Bonnin, Edith"],["dc.contributor.author","Cabochette, Pauline"],["dc.contributor.author","Filosa, Alessandro"],["dc.contributor.author","Jühlen, Ramona"],["dc.contributor.author","Komatsuzaki, Shoko"],["dc.contributor.author","Hezwani, Mohammed"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Martinelli, Valérie"],["dc.contributor.author","Vermeersch, Marjorie"],["dc.contributor.author","Supply, Lynn"],["dc.contributor.author","Martins, Nuno"],["dc.contributor.author","Pirenne, Laurence"],["dc.contributor.author","Ravenscroft, Gianina"],["dc.contributor.author","Lombard, Marcus"],["dc.contributor.author","Port, Sarah"],["dc.contributor.author","Spillner, Christiane"],["dc.contributor.author","Janssens, Sandra"],["dc.contributor.author","Roets, Ellen"],["dc.contributor.author","Van Dorpe, Jo"],["dc.contributor.author","Lammens, Martin"],["dc.contributor.author","Kehlenbach, Ralph H"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Laing, Nigel G"],["dc.contributor.author","Hoffmann, Katrin"],["dc.contributor.author","Vanhollebeke, Benoit"],["dc.contributor.author","Fahrenkrog, Birthe"],["dc.date.accessioned","2019-07-09T11:50:18Z"],["dc.date.available","2019-07-09T11:50:18Z"],["dc.date.issued","2018"],["dc.description.abstract","Nucleoporins build the nuclear pore complex (NPC), which, as sole gate for nuclear-cytoplasmic exchange, is of outmost importance for normal cell function. Defects in the process of nucleocytoplasmic transport or in its machinery have been frequently described in human diseases, such as cancer and neurodegenerative disorders, but only in a few cases of developmental disorders. Here we report biallelic mutations in the nucleoporin NUP88 as a novel cause of lethal fetal akinesia deformation sequence (FADS) in two families. FADS comprises a spectrum of clinically and genetically heterogeneous disorders with congenital malformations related to impaired fetal movement. We show that genetic disruption of nup88 in zebrafish results in pleiotropic developmental defects reminiscent of those seen in affected human fetuses, including locomotor defects as well as defects at neuromuscular junctions. Phenotypic alterations become visible at distinct developmental stages, both in affected human fetuses and in zebrafish, whereas early stages of development are apparently normal. The zebrafish phenotypes caused by nup88 deficiency are rescued by expressing wild-type Nup88 but not the disease-linked mutant forms of Nup88. Furthermore, using human and mouse cell lines as well as immunohistochemistry on fetal muscle tissue, we demonstrate that NUP88 depletion affects rapsyn, a key regulator of the muscle nicotinic acetylcholine receptor at the neuromuscular junction. Together, our studies provide the first characterization of NUP88 in vertebrate development, expand our understanding of the molecular events causing FADS, and suggest that variants in NUP88 should be investigated in cases of FADS."],["dc.identifier.doi","10.1371/journal.pgen.1007845"],["dc.identifier.pmid","30543681"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15905"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59742"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1553-7404"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","572"],["dc.subject.mesh","Alleles"],["dc.subject.mesh","Amino Acid Sequence"],["dc.subject.mesh","Animals"],["dc.subject.mesh","Animals, Genetically Modified"],["dc.subject.mesh","Arthrogryposis"],["dc.subject.mesh","Consanguinity"],["dc.subject.mesh","Disease Models, Animal"],["dc.subject.mesh","Female"],["dc.subject.mesh","Genes, Lethal"],["dc.subject.mesh","Humans"],["dc.subject.mesh","Male"],["dc.subject.mesh","Mice"],["dc.subject.mesh","Models, Molecular"],["dc.subject.mesh","Muscle Proteins"],["dc.subject.mesh","Mutation"],["dc.subject.mesh","Neuromuscular Junction"],["dc.subject.mesh","Nuclear Pore Complex Proteins"],["dc.subject.mesh","Pedigree"],["dc.subject.mesh","Pregnancy"],["dc.subject.mesh","Protein Conformation"],["dc.subject.mesh","Receptors, Nicotinic"],["dc.subject.mesh","Sequence Homology, Amino Acid"],["dc.subject.mesh","Zebrafish"],["dc.subject.mesh","Zebrafish Proteins"],["dc.title","Biallelic mutations in nucleoporin NUP88 cause lethal fetal akinesia deformation sequence"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","68"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","77"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Padmanabhan, Nirmala"],["dc.contributor.author","Fichtner, Lars"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Schulz, Joerg B."],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2017-09-07T11:47:35Z"],["dc.date.available","2017-09-07T11:47:35Z"],["dc.date.issued","2009"],["dc.description.abstract","Ynm3 is the only budding yeast protein possessing a combination of serine protease and postsynaptic density 95/disclarge/zona occludens domains, a defining feature of the high temperature requirement A (HtrA) protein family. The bacterial HtrA/DegP is involved in protective stress response to aid survival at higher temperatures. The role of mammalian mitochondrial HtrA2/Omi in protein quality control is unclear, although loss of its protease activity results in susceptibility toward Parkinson's disease, in which mitochondrial dysfunction and impairment of protein folding and degradation are key pathogenetic features. We studied the role of the budding yeast HtrA, Ynm3, with respect to unfolding stresses. Similar to Escherichia coli DegP, we find that Ynm3 is a dual chaperone-protease. Its proteolytic activity is crucial for cell survival at higher temperature. Ynm3 also exhibits strong general chaperone activity, a novel finding for a eukaryotic HtrA member. We propose that the chaperone activity of Ynm3 may be important to improve the efficiency of proteolysis of aberrant proteins by averting the formation of nonproductive toxic aggregates and presenting them in a soluble state to its protease domain. Suppression studies with Delta ynm3 led to the discovery of chaperone activity in a nucleolar peptidyl-prolyl cis-trans isomerase, Fpr3, which could partly relieve the heat sensitivity of Delta ynm3."],["dc.identifier.doi","10.1091/mbc.E08-02-0178"],["dc.identifier.gro","3143174"],["dc.identifier.isi","000262134800007"],["dc.identifier.pmid","18946088"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/5930"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/659"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Soc Cell Biology"],["dc.relation.issn","1059-1524"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","The Yeast HtrA Orthologue Ynm3 Is a Protease with Chaperone Activity that Aids Survival Under Heat Stress"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1507"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Biomolecules"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Perera, Roshan Priyarangana"],["dc.contributor.author","Shaikhqasem, Alaa"],["dc.contributor.author","Rostam, Nadia"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Tittmann, Kai"],["dc.contributor.author","Dosch, Roland"],["dc.date.accessioned","2021-12-01T09:22:46Z"],["dc.date.available","2021-12-01T09:22:46Z"],["dc.date.issued","2021"],["dc.description.abstract","Many multicellular organisms specify germ cells during early embryogenesis by the inheritance of ribonucleoprotein (RNP) granules known as germplasm. However, the role of complex interactions of RNP granules during germ cell specification remains elusive. This study characterizes the interaction of RNP granules, Buc, and zebrafish Vasa (zfVasa) during germ cell specification. We identify a novel zfVasa-binding motif (Buc-VBM) in Buc and a Buc-binding motif (zfVasa-BBM) in zfVasa. Moreover, we show that Buc and zfVasa directly bind in vitro and that this interaction is independent of the RNA. Our circular dichroism spectroscopy data reveal that the intrinsically disordered Buc-VBM peptide forms alpha-helices in the presence of the solvent trifluoroethanol. Intriguingly, we further demonstrate that Buc-VBM enhances zfVasa ATPase activity, thereby annotating the first biochemical function of Buc as a zfVasa ATPase activator. Collectively, these results propose a model in which the activity of zfVasa is a central regulator of primordial germ cell (PGC) formation and is tightly controlled by the germplasm organizer Buc."],["dc.description.abstract","Many multicellular organisms specify germ cells during early embryogenesis by the inheritance of ribonucleoprotein (RNP) granules known as germplasm. However, the role of complex interactions of RNP granules during germ cell specification remains elusive. This study characterizes the interaction of RNP granules, Buc, and zebrafish Vasa (zfVasa) during germ cell specification. We identify a novel zfVasa-binding motif (Buc-VBM) in Buc and a Buc-binding motif (zfVasa-BBM) in zfVasa. Moreover, we show that Buc and zfVasa directly bind in vitro and that this interaction is independent of the RNA. Our circular dichroism spectroscopy data reveal that the intrinsically disordered Buc-VBM peptide forms alpha-helices in the presence of the solvent trifluoroethanol. Intriguingly, we further demonstrate that Buc-VBM enhances zfVasa ATPase activity, thereby annotating the first biochemical function of Buc as a zfVasa ATPase activator. Collectively, these results propose a model in which the activity of zfVasa is a central regulator of primordial germ cell (PGC) formation and is tightly controlled by the germplasm organizer Buc."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.3390/biom11101507"],["dc.identifier.pii","biom11101507"],["dc.identifier.pmid","34680140"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94480"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/407"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","2218-273X"],["dc.relation.workinggroup","RG Ficner (Molecular Structural Biology)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Bucky Ball Is a Novel Zebrafish Vasa ATPase Activator"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]