Schendzielorz, Alexander Benjamin

[["dc.bibliographiccitation.firstpage","265"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Trends in Cell Biology"],["dc.bibliographiccitation.lastpage","275"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Schendzielorz, Alexander Benjamin"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:44:25Z"],["dc.date.available","2017-09-07T11:44:25Z"],["dc.date.issued","2015"],["dc.description.abstract","Trans location of presequence-containing precursor proteins into the inner mitochondrial membrane and matrix is an essential process that is facilitated by the translocase of the outer membrane (TOM) together with the presequence translocase of the inner membrane (TIM23). After initial recognition by receptors of the TOM complex followed by transport across the outer membrane, the precursor emerges into the intermembrane space (IMS). Recognition of the presequence by Tim50 triggers rearrangements of the presequence translocase, priming it for inner membrane translocation. Subsequently, the precursor can be released into the membrane or translocated into the mitochondrial matrix aided by the import motor. This heat-shock protein 70 (Hsp70)-based motor drives precursor unfolding and translocation and is subject to dynamic remodelling. Here, we review recent advances in understanding of the mechanisms underlying protein transport along the. presequence pathway."],["dc.identifier.doi","10.1016/j.tcb.2014.12.001"],["dc.identifier.gro","3141912"],["dc.identifier.isi","000353863700002"],["dc.identifier.pmid","25542066"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2456"],["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","0962-8924"],["dc.title","Unlocking the presequence import pathway"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1850"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],["dc.bibliographiccitation.lastpage","1859"],["dc.bibliographiccitation.volume","1853"],["dc.contributor.author","Melin, Jonathan"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Gomkale, Ridhima"],["dc.contributor.author","Schendzielorz, Alexander Benjamin"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Schulz, Christian"],["dc.date.accessioned","2017-09-07T11:43:40Z"],["dc.date.available","2017-09-07T11:43:40Z"],["dc.date.issued","2015"],["dc.description.abstract","The translocase of the outer mitochondrial membrane (TOM complex) is the general entry gate into mitochondria for almost all imported proteins. A variety of specific receptors allow the TOM complex to recognize targeting signals of various precursor proteins that are transported along different import pathways. Aside from the well-characterized presequence receptors Tom20 and Tom22 a third TOM receptor, Tom70, binds proteins of the carrier family containing multiple transmembrane segments. Here we demonstrate that Tom70 directly binds to presequence peptides using a dedicated groove. A single point mutation in the cavity of this pocket (M551R) reduces the presequence binding affinity of Tom70 ten-fold and selectively impairs import of the presequence-containing precursor Mdl1 but not the ADP/ATP carrier (MC). Hence Tom70 contributes to the presequence import pathway by recognition of the targeting signal of the Mdl1 precursor. (C) 2015 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.bbamcr.2015.04.021"],["dc.identifier.gro","3141858"],["dc.identifier.isi","000356209600009"],["dc.identifier.pmid","25958336"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1856"],["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","0006-3002"],["dc.relation.issn","0167-4889"],["dc.title","A presequence-binding groove in Tom70 supports import of Mdl1 into mitochondria"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","83"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","92"],["dc.bibliographiccitation.volume","216"],["dc.contributor.author","Schendzielorz, Alexander Benjamin"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Clancy, Anne"],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Ieva, Raffaele"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:53:21Z"],["dc.date.available","2017-09-07T11:53:21Z"],["dc.date.issued","2017"],["dc.description.abstract","wo driving forces energize precursor translocation across the inner mitochondrial membrane. Although the membrane potential (Δψ) is considered to drive translocation of positively charged presequences through the TIM23 complex (presequence translocase), the activity of the Hsp70-powered import motor is crucial for the translocation of the mature protein portion into the matrix. In this study, we show that mitochondrial matrix proteins display surprisingly different dependencies on the Δψ. However, a precursor's hypersensitivity to a reduction of the Δψ is not linked to the respective presequence, but rather to the mature portion of the polypeptide chain. The presequence translocase constituent Pam17 is specifically recruited by the receptor Tim50 to promote the transport of hypersensitive precursors into the matrix. Our analyses show that two distinct Δψ-driven translocation steps energize precursor passage across the inner mitochondrial membrane. The Δψ- and Pam17-dependent import step identified in this study is positioned between the two known energy-dependent steps: Δψ-driven presequence translocation and adenosine triphosphate-driven import motor activity."],["dc.identifier.doi","10.1083/jcb.201607066"],["dc.identifier.gro","3145078"],["dc.identifier.pmid","28011846"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2774"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/7"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.status","final"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | Z03: Synthetische genetische Analyse, automatisierte Mikroskopie und Bildanalyse"],["dc.relation.issn","0021-9525"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.rights","CC BY-NC-SA 4.0"],["dc.title","Two distinct membrane potential–dependent steps drive mitochondrial matrix protein translocation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]