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dc.contributor.authorBeddoe, T
dc.contributor.authorBushell, SR
dc.contributor.authorPerugini, MA
dc.contributor.authorLithgow, T
dc.contributor.authorMulhern, TD
dc.contributor.authorBottomley, SP
dc.contributor.authorRossjohn, J
dc.date.available2014-05-21T19:38:39Z
dc.date.issued2004-11-05
dc.identifierpii: S0021-9258(20)69851-9
dc.identifier.citationBeddoe, T., Bushell, S. R., Perugini, M. A., Lithgow, T., Mulhern, T. D., Bottomley, S. P. & Rossjohn, J. (2004). A biophysical analysis of the tetratricopeptide repeat-rich mitochondrial import receptor, Tom70, reveals an elongated monomer that is inherently flexible, unstable, and unfolds via a multistate pathway. JOURNAL OF BIOLOGICAL CHEMISTRY, 279 (45), pp.46448-46454. https://doi.org/10.1074/jbc.M405639200.
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/11343/26576
dc.descriptionC1 - Journal Articles Refereed
dc.description.abstractProteins destined for all submitochondrial compartments are translocated across the outer mitochondrial membrane by the TOM (translocase of the outer membrane) complex, which consists of a number of specialized receptor subunits that bind mitochondrial precursor proteins for delivery into the translocation channel. One receptor, Tom70, binds large, hydrophobic mitochondrial precursors. The current model of Tom70-mediated import involves multiple dimers of the receptor recognizing a single molecule of substrate. Here we show via a battery of biophysical and spectroscopic techniques that the cytosolic domain of Tom70 is an elongated monomer. Thermal and urea-induced denaturation revealed that the receptor, which unfolds via a multistate pathway, is a relatively unstable molecule undergoing major conformational change at physiological temperatures. The data suggest that the malleability of the monomeric Tom70 receptor is an important factor in mitochondrial import.
dc.formatapplication/pdf
dc.languageEnglish
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
dc.subjectBiochemistry and Cell Biology not elsewhere classified ; Biological Sciences
dc.titleA biophysical analysis of the tetratricopeptide repeat-rich mitochondrial import receptor, Tom70, reveals an elongated monomer that is inherently flexible, unstable, and unfolds via a multistate pathway
dc.typeJournal Article
dc.identifier.doi10.1074/jbc.M405639200
melbourne.peerreviewPeer Reviewed
melbourne.affiliationThe University of Melbourne
melbourne.affiliation.departmentBiochemistry And Molecular Biology
melbourne.source.titleJournal of Biological Chemistry
melbourne.source.volume279
melbourne.source.issue45
melbourne.source.pages46448-46454
melbourne.publicationid28403
melbourne.elementsid263229
melbourne.contributor.authorPerugini, Matthew
melbourne.contributor.authorLITHGOW, TREVOR
melbourne.contributor.authorMulhern, Terrence
dc.identifier.eissn1083-351X
melbourne.accessrightsThis item is currently not available from this repository


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