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A conserved proline residue is present in the transmembrane‐spanning domain of Tom7 and other tail‐anchored protein subunits of the TOM translocase
Author(s) -
Allen Renae,
Egan Billie,
Gabriel Kipros,
Beilharz Traude,
Lithgow Trevor
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02433-x
Subject(s) - translocase , integral membrane protein , transmembrane domain , transmembrane protein , translocase of the outer membrane , protein targeting , biochemistry , translocase of the inner membrane , membrane protein , biology , atp–adp translocase , proline , mitochondrial carrier , chemistry , microbiology and biotechnology , biophysics , amino acid , inner mitochondrial membrane , mitochondrial membrane transport protein , membrane , bacterial outer membrane , chromosomal translocation , receptor , gene , escherichia coli
The TOM translocase consists of several integral membrane proteins organised around the channel forming protein Tom40. Here we show that one of these protein subunits, Tom7, is a tail‐anchored protein. The carboxy‐terminal 33 amino acids of Tom7 contain the information for targeting the protein to the mitochondrial outer membrane, and a conserved proline residue within the transmembrane segment is required for efficient targeting of Tom7 to the outer membrane. An equivalent proline residue is important in targeting each of the other three tail‐anchored proteins that associate with Tom40 to form the core of the TOM translocase.