Reinhold, Robert

[["dc.bibliographiccitation.firstpage","3211"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Monthly Notices of the Royal Astronomical Society"],["dc.bibliographiccitation.lastpage","3226"],["dc.bibliographiccitation.volume","450"],["dc.contributor.author","Aigrain, S."],["dc.contributor.author","Llama, J."],["dc.contributor.author","Ceillier, T."],["dc.contributor.author","das Chagas, M. L."],["dc.contributor.author","Davenport, J. R. A."],["dc.contributor.author","Garcia, R. A."],["dc.contributor.author","Hay, K. L."],["dc.contributor.author","Lanza, A. F."],["dc.contributor.author","McQuillan, A."],["dc.contributor.author","Mazeh, T."],["dc.contributor.author","de Medeiros, J. R."],["dc.contributor.author","Nielsen, M. B."],["dc.contributor.author","Reinhold, T."],["dc.date.accessioned","2018-11-07T09:55:26Z"],["dc.date.available","2018-11-07T09:55:26Z"],["dc.date.issued","2015"],["dc.description.abstract","We present the results of a blind exercise to test the recoverability of stellar rotation and differential rotation in Kepler light curves. The simulated light curves lasted 1000 d and included activity cycles, Sun-like butterfly patterns, differential rotation and spot evolution. The range of rotation periods, activity levels and spot lifetime were chosen to be representative of the Kepler data of solar-like stars. Of the 1000 simulated light curves, 770 were injected into actual quiescent Kepler light curves to simulate Kepler noise. The test also included five 1000-d segments of the Sun's total irradiance variations at different points in the Sun's activity cycle. Five teams took part in the blind exercise, plus two teams who participated after the content of the light curves had been released. The methods used included Lomb-Scargle periodograms and variants thereof, autocorrelation function and wavelet-based analyses, plus spot modelling to search for differential rotation. The results show that the 'overall' period is well recovered for stars exhibiting low and moderate activity levels. Most teams reported values within 10 per cent of the true value in 70 per cent of the cases. There was, however, little correlation between the reported and simulated values of the differential rotation shear, suggesting that differential rotation studies based on full-disc light curves alone need to be treated with caution, at least for solar-type stars. The simulated light curves and associated parameters are available online for the community to test their own methods."],["dc.identifier.doi","10.1093/mnras/stv853"],["dc.identifier.isi","000356339300072"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36738"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","1365-2966"],["dc.relation.issn","0035-8711"],["dc.title","Testing the recovery of stellar rotation signals from Kepler light curves using a blind hare-and-hounds exercise"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5009"],["dc.bibliographiccitation.issue","24"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","5021"],["dc.bibliographiccitation.volume","32"],["dc.contributor.author","Reinhold, Robert"],["dc.contributor.author","Krüger, Vivien"],["dc.contributor.author","Meinecke, Michael"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Grunau, Silke D."],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Wiedemann, Nils"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Wagner, Richard"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Dudek, Jan"],["dc.date.accessioned","2017-09-07T11:48:21Z"],["dc.date.available","2017-09-07T11:48:21Z"],["dc.date.issued","2012"],["dc.description.abstract","The majority of multispanning inner mitochondrial membrane proteins utilize internal targeting signals, which direct them to the carrier translocase (TIM22 complex), for their import. MPV17 and its Saccharomyces cerevisiae orthologue Sym1 are multispanning inner membrane proteins of unknown function with an amino-terminal presequence that suggests they may be targeted to the mitochondria. Mutations affecting MPV17 are associated with mitochondrial DNA depletion syndrome (MDDS). Reconstitution of purified Sym1 into planar lipid bilayers and electrophysiological measurements have demonstrated that Sym1 forms a membrane pore. To address the biogenesis of Sym1, which oligomerizes in the inner mitochondrial membrane, we studied its import and assembly pathway. Sym1 forms a transport intermediate at the translocase of the outer membrane (TOM) complex. Surprisingly, Sym1 was not transported into mitochondria by an amino-terminal signal, and in contrast to what has been observed in carrier proteins, Sym1 transport and assembly into the inner membrane were independent of small translocase of mitochondrial inner membrane (TIM) and TIM22 complexes. Instead, Sym1 required the presequence of translocase for its biogenesis. Our analyses have revealed a novel transport mechanism for a polytopic membrane protein in which internal signals direct the precursor into the inner membrane via the TIM23 complex, indicating a presequence-independent function of this translocase."],["dc.identifier.doi","10.1128/MCB.00843-12"],["dc.identifier.gro","3142435"],["dc.identifier.isi","000311492200011"],["dc.identifier.pmid","23045398"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8252"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0270-7306"],["dc.title","The Channel-Forming Sym1 Protein Is Transported by the TIM23 Complex in a Presequence-Independent Manner"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4970"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","FEBS Journal"],["dc.bibliographiccitation.lastpage","4982"],["dc.bibliographiccitation.volume","280"],["dc.contributor.author","Welter, Evelyn"],["dc.contributor.author","Montino, Marco"],["dc.contributor.author","Reinhold, Robert"],["dc.contributor.author","Schlotterhose, Petra"],["dc.contributor.author","Krick, Roswitha"],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Thumm, Michael"],["dc.date.accessioned","2017-09-07T11:47:07Z"],["dc.date.available","2017-09-07T11:47:07Z"],["dc.date.issued","2013"],["dc.description.abstract","Mitochondria are turned over by an autophagic process termed mitophagy. This process is considered to remove damaged, superfluous and aged organelles. However, little is known about how defective organelles are recognized, what types of damage induce turnover, and whether an identical set of factors contributes to degradation under different conditions. Here we systematically compared the mitophagy rate and requirement for mitophagy-specific proteins during post-log-phase and rapamycin-induced mitophagy. To specifically assess mitophagy of damaged mitochondria, we analyzed cells accumulating proteins prone to degradation due to lack of the mitochondrial AAA-protease Yme1. While autophagy 32 (Atg32) was required under all tested conditions, the function of Atg33 could be partially bypassed in post-log-phase and rapamycin-induced mitophagy. Unexpectedly, we found that Uth1 was dispensable for mitophagy. A re-evaluation of its mitochondrial localization revealed that Uth1 is a protein of the inner mitochondrial membrane that is targeted by a cleavable N-terminal pre-sequence. In agreement with our functional analyses, this finding excludes a role of Uth1 as a mitochondrial surface receptor."],["dc.identifier.doi","10.1111/febs.12468"],["dc.identifier.gro","3142274"],["dc.identifier.isi","000327132100006"],["dc.identifier.pmid","23910823"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6465"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1742-4658"],["dc.relation.issn","1742-464X"],["dc.title","Uth1 is a mitochondrial inner membrane protein dispensable for post-log-phase and rapamycin-induced mitophagy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2379"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Human Molecular Genetics"],["dc.bibliographiccitation.lastpage","2393"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Reinhold, Robert"],["dc.contributor.author","Bareth, Bettina"],["dc.contributor.author","Balleininger, Martina"],["dc.contributor.author","Wissel, Mirjam"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Mick, David U."],["dc.date.accessioned","2017-09-07T11:44:14Z"],["dc.date.available","2017-09-07T11:44:14Z"],["dc.date.issued","2011"],["dc.description.abstract","Defects in mitochondrial energy metabolism lead to severe human disorders, mainly affecting tissues especially dependent on oxidative phosphorylation, such as muscle and brain. Leigh Syndrome describes a severe encephalomyopathy in infancy, frequently caused by mutations in SURF1. SURF1, termed Shy1 in Saccharomyces cerevisiae, is a conserved assembly factor for the terminal enzyme of the respiratory chain, cytochrome c oxidase. Although the molecular function of SURF1/Shy1 is still enigmatic, loss of function leads to cytochrome c oxidase deficiency and reduced expression of the central subunit Cox1 in yeast. Here, we provide insights into the molecular mechanisms leading to disease through missense mutations in codons of the most conserved amino acids in SURF1. Mutations affecting G(124) do not compromise import of the SURF1 precursor protein but lead to fast turnover of the mature protein within the mitochondria. Interestingly, an (YD)-D-274 exchange neither affects stability nor localization of the protein. Instead, SURF1(Y274D) accumulates in a 200 kDa cytochrome c oxidase assembly intermediate. Using yeast as a model, we demonstrate that the corresponding Shy1(Y344D) is able to overcome the stage where cytochrome c oxidase assembly links to the feedback regulation of mitochondrial Cox1 expression. However, Shy1(Y344D) impairs the assembly at later steps, most apparent at low temperature and exhibits a dominant-negative phenotype upon overexpression. Thus, exchanging the conserved tyrosine (Y-344) with aspartate in yeast uncouples translational regulation of Cox1 from cytochrome c oxidase assembly and provides evidence for the dual functionality of Shy1."],["dc.identifier.doi","10.1093/hmg/ddr145"],["dc.identifier.gro","3142715"],["dc.identifier.isi","000290849200008"],["dc.identifier.pmid","21470975"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/150"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1460-2083"],["dc.relation.issn","0964-6906"],["dc.title","Mimicking a SURF1 allele reveals uncoupling of cytochrome c oxidase assembly from translational regulation in yeast"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1528"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","1541"],["dc.bibliographiccitation.volume","151"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Wiese, Heike"],["dc.contributor.author","Reinhold, Robert"],["dc.contributor.author","Pacheu-Grau, David"],["dc.contributor.author","Lorenzi, Isotta"],["dc.contributor.author","Sasarman, Florin"],["dc.contributor.author","Weraarpachai, Woranontee"],["dc.contributor.author","Shoubridge, Eric A."],["dc.contributor.author","Warscheid, Bettina"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:48:20Z"],["dc.date.available","2017-09-07T11:48:20Z"],["dc.date.issued","2012"],["dc.description.abstract","Mitochondrial respiratory-chain complexes assemble from subunits of dual genetic origin assisted by specialized assembly factors. Whereas core subunits are translated on mitochondrial ribosomes, others are imported after cytosolic translation. How imported subunits are ushered to assembly intermediates containing mitochondria-encoded subunits is unresolved. Here, we report a comprehensive dissection of early cytochrome c oxidase assembly intermediates containing proteins required for normal mitochondrial translation and reveal assembly factors promoting biogenesis of human respiratory-chain complexes. We find that TIM21, a subunit of the inner-membrane presequence translocase, is also present in the major assembly intermediates containing newly mitochondria-synthesized and imported respiratory-chain subunits, which we term MITRAC complexes. Human TIM21 is dispensable for protein import but required for integration of early-assembling, presequence-containing subunits into respiratory-chain intermediates. We establish an unexpected molecular link between the TIM23 transport machinery and assembly of respiratory-chain complexes that regulate mitochondrial protein synthesis in response to their assembly state."],["dc.identifier.doi","10.1016/j.cell.2012.11.053"],["dc.identifier.gro","3142426"],["dc.identifier.isi","000312890300017"],["dc.identifier.pmid","23260140"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8152"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0092-8674"],["dc.title","MITRAC Links Mitochondrial Protein Translocation to Respiratory-Chain Assembly and Translational Regulation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]