In vivo protein-interaction mapping of a mitochondrial translocator protein Tom22 at work

Takuya Shiota, Hide Mabuchi, Sachiko Tanaka-Yamano, Koji Yamano, Toshiya Endo

Research output: Contribution to journalArticleResearchpeer-review

78 Citations (Scopus)

Abstract

Mitochondrial protein import requires cooperation of the machineries called translocators in the outer and inner mitochondrial membranes. Here we analyze the interactions of Tom22, a multifunctional subunit of the outer membrane translocator TOM40 complex, with other translocator subunits such as Tom20, Tom40, and Tim50 and with substrate precursor proteins at a spatial resolution of the amino acid residue by in vivo and in organello site-specific photocross-linking. Changes in cross-linking patterns caused by excess substrate precursor proteins or presequence peptides indicate how the cytosolic receptor domain of Tom22 accepts substrate proteins and how the intermembrane space domain of Tom22 transfers them to Tim50 of the inner-membrane translocator.

Original languageEnglish
Pages (from-to)15179-15183
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume108
Issue number37
DOIs
Publication statusPublished - 13 Sep 2011
Externally publishedYes

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