Evolution of Peptidase Diversity

被引:80
作者
Page, Michael J. [1 ]
Di Cera, Enrico [1 ]
机构
[1] Washington Univ, Sch Med, Dept Biochem & Mol Biophys, St Louis, MO 63110 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1074/jbc.M804650200
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
A wide variety of peptidases associate with vital biological pathways, but the origin and evolution of their tremendous diversity are poorly defined. Application of the MEROPS classification to a comprehensive set of genomes yields a simple pattern of peptidase distribution and provides insight into the organization of proteolysis in all forms of life. Unexpectedly, a near ubiquitous core set of peptidases is shown to contain more types than those unique to higher multicellular organisms. From this core group, an array of eukaryote-specific peptidases evolved to yield well known intracellular and extracellular processes. The paucity of peptidase families unique to higher metazoa suggests gains in proteolytic network complexity required a limited number of biochemical inventions. These findings provide a framework for deeper investigation into the evolutionary forces that shaped each peptidase family and a roadmap to develop a time-line for their expansion as an interconnected system.
引用
收藏
页码:30010 / 30014
页数:5
相关论文
共 58 条
[1]   Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches [J].
Aravind, L ;
Koonin, EV .
JOURNAL OF MOLECULAR BIOLOGY, 1999, 287 (05) :1023-1040
[2]   'Species' of peptidases [J].
Barrett, Alan J. ;
Rawlings, Neil D. .
BIOLOGICAL CHEMISTRY, 2007, 388 (11) :1151-1157
[3]   AN UNUSUAL ACTIVE-SITE IDENTIFIED IN A FAMILY OF ZINC METALLOENDOPEPTIDASES [J].
BECKER, AB ;
ROTH, RA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (09) :3835-3839
[4]   Innate immunity: an overview [J].
Beutler, B .
MOLECULAR IMMUNOLOGY, 2004, 40 (12) :845-859
[5]   A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells [J].
Black, RA ;
Rauch, CT ;
Kozlosky, CJ ;
Peschon, JJ ;
Slack, JL ;
Wolfson, MF ;
Castner, BJ ;
Stocking, KL ;
Reddy, P ;
Srinivasan, S ;
Nelson, N ;
Boiani, N ;
Schooley, KA ;
Gerhart, M ;
Davis, R ;
Fitzner, JN ;
Johnson, RS ;
Paxton, RJ ;
March, CJ ;
Cerretti, DP .
NATURE, 1997, 385 (6618) :729-733
[6]   Mutational analysis of the proteolytic domain of pregnancy-associated plasma protein-A (PAPP-A): classification as a metzincin [J].
Boldt, HB ;
Overgaard, MT ;
Laursen, LS ;
Weyer, K ;
Sottrup-Jensen, L ;
Oxvig, C .
BIOCHEMICAL JOURNAL, 2001, 358 (02) :359-367
[7]   A PROTEIN CATALYTIC FRAMEWORK WITH AN N-TERMINAL NUCLEOPHILE IS CAPABLE OF SELF-ACTIVATION [J].
BRANNIGAN, JA ;
DODSON, G ;
DUGGLEBY, HJ ;
MOODY, PCE ;
SMITH, JL ;
TOMCHICK, DR ;
MURZIN, AG .
NATURE, 1995, 378 (6555) :416-419
[8]   The phagotrophic origin of eukaryotes and phylogenetic classification of protozoa [J].
Cavalier-Smith, T .
INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY, 2002, 52 :297-354
[9]   Caspases: the executioners of apoptosis [J].
Cohen, GM .
BIOCHEMICAL JOURNAL, 1997, 326 :1-16
[10]   Structure and functions of the 20S and 26S proteasomes [J].
Coux, O ;
Tanaka, K ;
Goldberg, AL .
ANNUAL REVIEW OF BIOCHEMISTRY, 1996, 65 :801-847