Preprotein translocase of the outer mitochondrial membrane: Reconstituted Tom40 forms a characteristic TOM pore

DC FieldValueLanguage
dc.contributor.authorBecker, L
dc.contributor.authorBannwarth, M
dc.contributor.authorMeisinger, C
dc.contributor.authorHill, K
dc.contributor.authorModel, K
dc.contributor.authorKrimmer, T
dc.contributor.authorCasadio, R
dc.contributor.authorTruscott, KN
dc.contributor.authorSchulz, GE
dc.contributor.authorPfanner, N
dc.contributor.authorWagner, R
dc.date.accessioned2021-12-23T16:16:13Z-
dc.date.available2021-12-23T16:16:13Z-
dc.date.issued2005
dc.identifier.issn00222836
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/11775-
dc.description.abstractTom40 is the central pore-forming component of the translocase of the outer mitochondrial membrane (TOM complex). Different views exist about the secondary structure and electrophysiological characteristics of Tom40 from Saccharomyces cerevisiae and Neurospora crassa. We have directly compared expressed and renatured Tom40 from both species and find a high content of beta-structure in circular dichroism measurements in agreement with refined secondary structure predictions. The electrophysiological characterization of renatured Torn,40 reveals the same characteristics as the purified TOM complex or mitochondrial outer membrane vesicles, with two exceptions. The total conductance of the TOM complex and outer membrane vesicles is twofold higher than the total conductance of renatured Tom40, consistent with the presence of two TOM pores. TOM complex and outer membrane vesicles possess a strongly enhanced sensitivity to a mitochondrial presequence compared to Tom40 alone, in agreement with the presence of several presequence binding sites in the TOM complex, suggesting a role of the non-channel Tom proteins in regulating channel activity. (c) 2005 Elsevier Ltd. All rights reserved.
dc.language.isoen
dc.publisherACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
dc.relation.ispartofJOURNAL OF MOLECULAR BIOLOGY
dc.subjectBETA
dc.subjectBiochemistry & Molecular Biology
dc.subjectCIRCULAR-DICHROISM SPECTRA
dc.subjectCOMPLEX
dc.subjectCOMPONENT
dc.subjectCORE
dc.subjectINSERTION
dc.subjectmitochondria
dc.subjectNeurospora crassa
dc.subjectPROTEIN IMPORT CHANNEL
dc.subjectprotein sorting
dc.subjectRECEPTORS
dc.subjectRECOGNITION
dc.subjectREGIONS
dc.subjectSaccharomyces cerevisiae
dc.subjectTOM complex
dc.titlePreprotein translocase of the outer mitochondrial membrane: Reconstituted Tom40 forms a characteristic TOM pore
dc.typejournal article
dc.identifier.doi10.1016/j.jmb.2005.09.019
dc.identifier.isiISI:000233206700009
dc.description.volume353
dc.description.issue5
dc.description.startpage1011
dc.description.endpage1020
dc.contributor.orcid0000-0002-8326-3548
dc.contributor.orcid0000-0002-7462-7039
dc.contributor.orcid0000-0002-5352-9835
dc.contributor.researcheridD-3362-2012
dc.contributor.researcheridJ-1110-2014
dc.contributor.researcheridK-3747-2017
dc.contributor.researcheridAAV-7878-2021
dc.contributor.researcheridK-4814-2015
dc.identifier.eissn10898638
dc.publisher.place24-28 OVAL RD, LONDON NW1 7DX, ENGLAND
dcterms.isPartOf.abbreviationJ. Mol. Biol.
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidWaRi703-
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