Evolution and disorder

被引:214
作者
Brown, Celeste J. [1 ]
Johnson, Audra K. [1 ]
Dunker, A. Keith [2 ,3 ]
Daughdrill, Gary W. [4 ]
机构
[1] Univ Idaho, Dept Biol Sci, IBEST, Moscow, ID 83844 USA
[2] Indiana Univ Sch Med, Ctr Computat Biol & Bioinformat Biochem & Mol Bio, Indianapolis, IN 46202 USA
[3] Indiana Univ, Ctr Computat Biol & Bioinformat Biochem & Mol Bio, Sch Dent, Indianapolis, IN 46202 USA
[4] Univ S Florida, Dept Cell Biol Microbiol & Mol Biol, Ctr Drug Discovery & Innovat, Tampa, FL 33612 USA
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
UNSTRUCTURED TRANSACTIVATION DOMAIN; INTRINSIC DISORDER; UNFOLDED PROTEINS; BINDING; SEQUENCE; CONSERVATION; MECHANISM; FAMILIES; DATABASE; EVOLVE;
D O I
10.1016/j.sbi.2011.02.005
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 evolution of disordered proteins or regions of proteins differs from that of ordered proteins because of the differences in their sequence composition, intramolecular contacts, and function. Recent assessments of disordered protein evolution at the sequence, structural, and functional levels support this hypothesis. Disordered proteins have a different pattern of accepted point mutations, exhibit higher rates of insertions and deletions, and generally, but not always, evolve more rapidly than ordered proteins. Even with these high rates of sequence evolution, a few examples have shown that disordered proteins maintain their flexibility under physiological conditions, and it is hypothesized that they maintain specific structural ensembles.
引用
收藏
页码:441 / 446
页数:6
相关论文
共 55 条
[1]   The Myofibrillar Protein, Projectin, is Highly Conserved Across Insect Evolution Except for Its PEVK Domain [J].
Ayme-Southgate, Agnes J. ;
Southgate, Richard J. ;
Philipp, Richard A. ;
Sotka, Erik E. ;
Kramp, Catherine .
JOURNAL OF MOLECULAR EVOLUTION, 2008, 67 (06) :653-669
[2]   Defining long-range order and local disorder in native α-synuclein using residual dipolar couplings [J].
Bernadó, P ;
Bertoncini, CW ;
Griesinger, C ;
Zweckstetter, M ;
Blackledge, M .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (51) :17968-17969
[3]   A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering [J].
Bernadó, P ;
Blanchard, L ;
Timmins, P ;
Marion, D ;
Ruigrok, RWH ;
Blackledge, M .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (47) :17002-17007
[4]   Comparing Models of Evolution for Ordered and Disordered Proteins [J].
Brown, Celeste J. ;
Johnson, Audra K. ;
Daughdrill, Gary W. .
MOLECULAR BIOLOGY AND EVOLUTION, 2010, 27 (03) :609-621
[5]   Evolutionary rate heterogeneity in proteins with long disordered regions [J].
Brown, CJ ;
Takayama, S ;
Campen, AM ;
Vise, P ;
Marshall, TW ;
Oldfield, CJ ;
Williams, CJ ;
Dunker, AK .
JOURNAL OF MOLECULAR EVOLUTION, 2002, 55 (01) :104-110
[6]   Conservation of intrinsic disorder in protein domains and families: I. A database of conserved predicted disordered regions [J].
Chen, JW ;
Romero, P ;
Uversky, VN ;
Dunker, AK .
JOURNAL OF PROTEOME RESEARCH, 2006, 5 (04) :879-887
[7]   Conservation of intrinsic disorder in protein domains and families: II. Functions of conserved disorder [J].
Chen, JW ;
Romero, P ;
Uversky, VN ;
Dunker, AK .
JOURNAL OF PROTEOME RESEARCH, 2006, 5 (04) :888-898
[8]   Phosphorylated and Nonphosphorylated Serine and Threonine Residues Evolve at Different Rates in Mammals [J].
Chen, Sean Chun-Chang ;
Chen, Feng-Chi ;
Li, Wen-Hsiung .
MOLECULAR BIOLOGY AND EVOLUTION, 2010, 27 (11) :2548-2554
[9]   Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation [J].
Daughdrill, Gary W. ;
Narayanaswami, Pranesh ;
Gilmore, Sara H. ;
Belczyk, Agniezka ;
Brown, Celeste J. .
JOURNAL OF MOLECULAR EVOLUTION, 2007, 65 (03) :277-288
[10]  
DAUGHDRILL GW, 2005, HDB PROTEIN FOLDING, V2, P275