Structural characterization of the Get4/Get5 complex and its interaction with Get3

被引：69

作者：

Chartron, Justin W. ^{[1
]}

Suloway, Christian J. M. ^{[1
]}

Zaslaver, Ma'ayan ^{[1
]}

Clemons, William M., Jr. ^{[1
]}

机构：

[1] CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2010年 / 107卷 / 27期

基金：

美国国家卫生研究院;

关键词：

crystallography; Get pathway; Mdy2; Ubl4a; tail-anchor; TAIL-ANCHORED PROTEINS; MEMBRANE INSERTION; YEAST; IDENTIFICATION; LANDSCAPE; BINDING; PATHWAY; MODEL;

D O I：

10.1073/pnas.1006036107

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The recently elucidated Get proteins are responsible for the targeted delivery of the majority of tail-anchored (TA) proteins to the endoplasmic reticulum. Get4 and Get5 have been identified in the early steps of the pathway mediating TA substrate delivery to the cytoplasmic targeting factor Get3. Here we report a crystal structure of Get4 and an N-terminal fragment of Get5 from Saccharomyces cerevisae. We show Get4 and Get5 (Get4/5) form an intimate complex that exists as a dimer (two copies of Get4/5) mediated by the C-terminus of Get5. We further demonstrate that Get3 specifically binds to a conserved surface on Get4 in a nucleotide dependent manner. This work provides further evidence for a model in which Get4/5 operates upstream of Get3 and mediates the specific delivery of a TA substrate.

引用

页码：12127 / 12132

页数：6

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