Premium
Signal recognition initiates reorganization of the presequence translocase during protein import
Author(s) -
Lytovchenko Oleksandr,
Melin Jonathan,
Schulz Christian,
Kilisch Markus,
Hutu Dana P,
Rehling Peter
Publication year - 2013
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2013.23
Subject(s) - translocase , intermembrane space , biology , translocase of the inner membrane , translocase of the outer membrane , microbiology and biotechnology , transport protein , protein targeting , mitochondrial intermembrane space , mitochondrion , atp–adp translocase , biochemistry , inner mitochondrial membrane , mitochondrial membrane transport protein , membrane protein , bacterial outer membrane , chromosomal translocation , gene , membrane , escherichia coli
The mitochondrial presequence translocase interacts with presequence‐containing precursors at the intermembrane space (IMS) side of the inner membrane to mediate their translocation into the matrix. Little is known as too how these matrix‐targeting signals activate the translocase in order to initiate precursor transport. Therefore, we analysed how signal recognition by the presequence translocase initiates reorganization among Tim‐proteins during import. Our analyses revealed that the presequence receptor Tim50 interacts with Tim21 in a signal‐sensitive manner in a process that involves the IMS‐domain of the Tim23 channel. The signal‐driven release of Tim21 from Tim50 promotes recruitment of Pam17 and thus triggers formation of the motor‐associated form of the TIM23 complex required for matrix transport.