Cold stability of intrinsically disordered proteins

被引：42

作者：

Tantos, Agnes ^{[1
]}

Friedrich, Peter ^{[1
]}

Tompa, Peter ^{[1
]}

机构：

[1] Hungarian Acad Sci, Inst Enzymol, Biol Res Ctr, H-1113 Budapest, Hungary

来源：

FEBS LETTERS | 2009年 / 583卷 / 02期

基金：

匈牙利科学研究基金会;

关键词：

Cold denaturation; Cold shock protein; LEA; Intrinsically disordered protein; Chaperone; Stability; UNSTRUCTURED PROTEINS; ARABIDOPSIS-THALIANA; STRUCTURAL DISORDER; MOLECULAR-BASIS; CALPASTATIN; ADAPTATION; CALPAIN; STRESS; DENATURATION; CHAPERONES;

D O I：

10.1016/j.febslet.2008.12.054

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：

Contrary to globular proteins, intrinsically disordered proteins (IDPs) lack a folded structure and they do not lose solubility at elevated temperatures. Although this should also be true at low temperatures, cold stability of IDPs has not been addressed in any scientific work so far. As direct characterization of cold-denaturation is difficult, we approached the problem through a freezing-induced loss-of-function model of globular-disordered functional protein pairs (m-calpain-calpastatin, tubulin-Map2c, Hsp90-ERD14). Our results affirm that in contrast with globular proteins IDPs are resistant to cold treatment. The theoretical and functional aspects of this observation are discussed. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：465 / 469

页数：5

共 37 条

[1] Cryoprotective activity of a cold-induced dehydrin purified from barley [J].

Bravo, LA ;

Gallardo, J ;

Navarrete, A ;

Olave, N ;

Martínez, J ;

Alberdi, M ;

Close, TJ ;

Corcuera, LJ .

PHYSIOLOGIA PLANTARUM, 2003, 118 (02) :262-269

[2] Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein [J].

Chandrayan, Sanjeev Kumar ;

Guptasarma, Purnananda .

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2008, 72 (02) :539-546

[3] Primary contact sites in intrinsically unstructured proteins:: The case of calpastatin and microtubule-associated protein 2 [J].

Csizmók, V ;

Bokor, M ;

Bánki, P ;

Klement, T ;

Medzihradszky, KF ;

Friedrich, P ;

Tompa, K ;

Tompa, P .

BIOCHEMISTRY, 2005, 44 (10) :3955-3964

[4] Psychrophilic microorganisms: challenges for life [J].

D'Amico, S ;

Collins, T ;

Marx, JC ;

Feller, G ;

Gerday, C .

EMBO REPORTS, 2006, 7 (04) :385-389

[5] Molecular basis of cold adaptation [J].

D'Amico, S ;

Claverie, P ;

Collins, T ;

Georlette, D ;

Gratia, E ;

Hoyoux, A ;

Meuwis, MA ;

Feller, G ;

Gerday, C .

PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES, 2002, 357 (1423) :917-924

[6] Adaptation of model proteins from cold to hot environments involves continuous and small adjustments of average parameters related to amino acid composition [J].

de Vendittis, Emmanuele ;

Castellano, Immacolata ;

Cotugno, Roberta ;

Ruocco, Maria Rosaria ;

Raimo, Gennaro ;

Masullo, Mariorosario .

JOURNAL OF THEORETICAL BIOLOGY, 2008, 250 (01) :156-171

[7] IUPred:: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content [J].

Dosztányi, Z ;

Csizmok, V ;

Tompa, P ;

Simon, I .

BIOINFORMATICS, 2005, 21 (16) :3433-3434

[8] Tubulin and microtubule structure [J].

Downing, KH ;

Nogales, E .

CURRENT OPINION IN CELL BIOLOGY, 1998, 10 (01) :16-22

[9] Intrinsically disordered protein [J].

Dunker, AK ;

Lawson, JD ;

Brown, CJ ;

Williams, RM ;

Romero, P ;

Oh, JS ;

Oldfield, CJ ;

Campen, AM ;

Ratliff, CR ;

Hipps, KW ;

Ausio, J ;

Nissen, MS ;

Reeves, R ;

Kang, CH ;

Kissinger, CR ;

Bailey, RW ;

Griswold, MD ;

Chiu, M ;

Garner, EC ;

Obradovic, Z .

JOURNAL OF MOLECULAR GRAPHICS & MODELLING, 2001, 19 (01) :26-59

[10] Intrinsically unstructured proteins and their functions [J].

Dyson, HJ ;

Wright, PE .

NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2005, 6 (03) :197-208

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