A conserved proline residue is present in the transmembrane-spanning domain of Tom7 and other tail-anchored protein subunits of the TOM translocase

Renae Allen, Billie Egan, Kip Gabriel, Traude Beilharz, Trevor James Lithgow

Research output: Contribution to journalArticleResearchpeer-review

39 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)347 - 350
Number of pages4
JournalFEBS Letters
Volume514
Issue number2-3
Publication statusPublished - 2002

Cite this

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title = "A conserved proline residue is present in the transmembrane-spanning domain of Tom7 and other tail-anchored protein subunits of the TOM translocase",
abstract = "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.",
author = "Renae Allen and Billie Egan and Kip Gabriel and Traude Beilharz and Lithgow, {Trevor James}",
year = "2002",
language = "English",
volume = "514",
pages = "347 -- 350",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Wiley-Blackwell",
number = "2-3",

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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. / Allen, Renae; Egan, Billie; Gabriel, Kip; Beilharz, Traude; Lithgow, Trevor James.

In: FEBS Letters, Vol. 514, No. 2-3, 2002, p. 347 - 350.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - A conserved proline residue is present in the transmembrane-spanning domain of Tom7 and other tail-anchored protein subunits of the TOM translocase

AU - Allen, Renae

AU - Egan, Billie

AU - Gabriel, Kip

AU - Beilharz, Traude

AU - Lithgow, Trevor James

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

UR - http://www.sciencedirect.com/science?

M3 - Article

VL - 514

SP - 347

EP - 350

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 2-3

ER -