A distinct structural region of the prokaryotic ubiquitin-like protein (Pup) is recognized by the N-terminal domain of the proteasomal ATPase Mpa

被引：79

作者：

Sutter, Markus ^{[1
]}

Striebel, Frank ^{[1
]}

Damberger, Fred F. ^{[1
]}

Allain, Frederic H. -T. ^{[1
]}

Weber-Ban, Eilika ^{[1
]}

机构：

[1] ETH, Inst Mol Biol & Biophys, CH-8093 Zurich, Switzerland

来源：

FEBS LETTERS | 2009年 / 583卷 / 19期

基金：

瑞士国家科学基金会;

关键词：

Prokaryotic ubiquitin-like protein; Mpa; ARC; Proteasome; NMR; Mycobacterium tuberculosis; MYCOBACTERIUM-TUBERCULOSIS; IDENTIFICATION; RHODOCOCCUS; NMR;

D O I：

10.1016/j.febslet.2009.09.020

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The mycobacterial ubiquitin-like protein Pup is coupled to proteins, thereby rendering them as substrates for proteasome-mediated degradation. The Pup-tagged proteins are recruited by the proteasomal ATPase Mpa (also called ARC). Using a combination of biochemical and NMR methods, we characterize the structural determinants of Pup and its interaction with Mpa, demonstrating that Pup adopts a range of extended conformations with a short helical stretch in its C-terminal portion. We show that the N-terminal coiled-coil domain of Mpa makes extensive contacts along the central region of Pup leaving its N-terminus unconstrained and available for other functional interactions. Structured summary: MINT-7262427:pup (uniprotkb:B6DAC1) binds (MI:0407) to mpa (uniprotkb:Q0G9Y7) by pull down (MI:0096) MINT-7262440:mpa (uniprotkb:Q0G9Y7) and pup (uniprotkb:B6DAC1) bind (MI:0407) by isothermal titration calorimetry (MI:0065) (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：3151 / 3157

页数：7

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