Domain organization of the monomeric form of the Tom70 mitochondrial import receptor

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dc.contributor.authorMills, RDen_AU
dc.contributor.authorTrewhella, Jen_AU
dc.contributor.authorQiu, TWen_AU
dc.contributor.authorWelte, Ten_AU
dc.contributor.authorRyan, TMen_AU
dc.contributor.authorHanley, TLen_AU
dc.contributor.authorKnott, RBen_AU
dc.contributor.authorLithgow, Ten_AU
dc.contributor.authorMulhern, TDen_AU
dc.date.accessioned2009-09-30T01:52:33Zen_AU
dc.date.accessioned2010-04-30T05:04:23Zen_AU
dc.date.available2009-09-30T01:52:33Zen_AU
dc.date.available2010-04-30T05:04:23Zen_AU
dc.date.issued2009-05-22en_AU
dc.date.statistics2009-05-22en_AU
dc.description.abstractTom70 is a mitochondrial protein import receptor composed of 11 tetratricopeptide repeats (TPRs). The first three TPRs form an N-terminal domain that recruits heat shock protein family chaperones, while the eight C-terminal TPRs form a domain that receives, from the bound chaperone, mitochondrial precursor proteins destined for import. Analytical Ultracentrifugation and solution small-angle X-ray scattering (SAXS) analysis characterized Tom70 as an elongated monomer. A model for the Tom70 monomer was proposed based on the alternate interpretation of the domain pairings observed in the crystal structure of the Tom70 dimer and refined against the SAXS data. In this "open" model of the Tom70 monomer, the chaperone- and precursor-binding sites are exposed and lay side by side oil one face of the molecule. Fluorescence anisotropy measurements indicated that monomeric Tom70 can bind both chaperone and precursor peptides and that chaperone peptide binding does not alter the affinity of Tom70 for the precursor peptide. SAXS Was unable to detect any shape change in Tom70 upon chaperone binding. However, molecular modeling indicated that chaperone binding is incompatible with Tom70 dimer formation. It is proposed that the Tom70 monomer is the functional unit mediating initial chaperone docking and precursor recognition. © 2009, Elsevier Ltd.en_AU
dc.identifier.citationMills, R. D., Trewhella, J., Qiu, T. W., Welte, T., Ryan, T. M., Hanley, T., Knott, R. B., Lithgow, T. & Mulhern, T. D. (2009). Domain organization of the monomeric form of the Tom70 mitochondrial import receptor. Journal of Molecular Biology, 388(5), 1043-1058. doi:10.1016/j.jmb.2009.03.070en_AU
dc.identifier.govdoc1284en_AU
dc.identifier.issn0022-2836en_AU
dc.identifier.issue5en_AU
dc.identifier.journaltitleJournal of Molecular Biologyen_AU
dc.identifier.pagination1043-1058en_AU
dc.identifier.urihttp://dx.doi.org/10.1016/j.jmb.2009.03.070en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/1876en_AU
dc.identifier.volume388en_AU
dc.language.isoenen_AU
dc.publisherElsevieren_AU
dc.subjectProtein structureen_AU
dc.subjectReceptorsen_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectDomain structureen_AU
dc.subjectMolecular modelsen_AU
dc.subjectPeptidesen_AU
dc.titleDomain organization of the monomeric form of the Tom70 mitochondrial import receptoren_AU
dc.typeJournal Articleen_AU
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