An abundance of bacterial ADP-ribosyltransferases - implications for the origin of exotoxins and their human homologues

被引：52

作者：

Pallen, MJ ^{[1
]}

Lam, AC

Loman, NJ

McBride, A

机构：

[1] Univ Birmingham, Div Immun & Infect, Microbial Genomics & Pathogenesis Unit, Sch Med, Birmingham B15 2TT, W Midlands, England

[2] Queens Univ Belfast, Dept Microbiol & Immunobiol, Belfast BT12 6BN, Antrim, North Ireland

来源：

TRENDS IN MICROBIOLOGY | 2001年 / 9卷 / 07期

关键词：

D O I：

10.1016/S0966-842X(01)02074-1

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：

ADP-ribosylation is a post-translational modification that can be seen in many contexts, including as the primary mechanism of action of many important bacterial exotoxins, By data-mining complete and incomplete bacterial genome sequences, we have discovered > 20 novel putative ADP-ribosyltransferases. including several new potential toxins.

引用

页码：302 / 307

页数：6

共 34 条

[1] The Pseudomonas syringae Hrp pathogenicity island has a tripartite mosaic structure composed of a cluster of type III secretion genes bounded by exchangeable effector and conserved effector loci that contribute to parasitic fitness and pathogenicity in plants [J].

Alfano, JR ;

Charkowski, AO ;

Deng, WL ;

Badel, JL ;

Petnicki-Ocwieja, T ;

van Dijk, K ;

Collmer, A .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (09) :4856-4861

[2] Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].

Altschul, SF ;

Madden, TL ;

Schaffer, AA ;

Zhang, JH ;

Zhang, Z ;

Miller, W ;

Lipman, DJ .

NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402

[3]

ANTOINE R, 1994, J BIOL CHEM, V269, P6450

[4]

Bazan JF, 1997, ADV EXP MED BIOL, V419, P99

[5] AB(5) ADP-RIBOSYLATING TOXINS - COMPARATIVE ANATOMY AND PHYSIOLOGY [J].

BURNETTE, WN .

STRUCTURE, 1994, 2 (03) :151-158

[6] Re-annotating the Mycoplasma pneumoniae genome sequence:: adding value, function and reading frames [J].

Dandekar, T ;

Huynen, M ;

Regula, JT ;

Ueberle, B ;

Zimmermann, CU ;

Andrade, MA ;

Doerks, T ;

Sánchez-Pulido, L ;

Snel, B ;

Suyama, M ;

Yuan, YP ;

Herrmann, R ;

Bork, P .

NUCLEIC ACIDS RESEARCH, 2000, 28 (17) :3278-3288

[7] Three conserved consensus sequences identify the NAD-binding site of ADP-ribosylating enzymes, expressed by eukaryotes, bacteria and T-even bacteriophages [J].

Domenighini, M ;

Rappuoli, R .

MOLECULAR MICROBIOLOGY, 1996, 21 (04) :667-674

[8] COMMON FEATURES OF THE NAD-BINDING AND CATALYTIC SITE OF ADP-RIBOSYLATING TOXINS [J].

DOMENIGHINI, M ;

MAGAGNOLI, C ;

PIZZA, M ;

RAPPUOLI, R .

MOLECULAR MICROBIOLOGY, 1994, 14 (01) :41-50

[9] DEMONSTRATION AND PARTIAL CHARACTERIZATION OF ADP-RIBOSYLATION IN PSEUDOMONAS-MALTOPHILIA [J].

EDMONDS, C ;

GRIFFIN, GE ;

JOHNSTONE, AP .

BIOCHEMICAL JOURNAL, 1989, 261 (01) :113-118

[10] Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex [J].

Han, S ;

Craig, JA ;

Putnam, CD ;

Carozzi, NB ;

Tainer, JA .

NATURE STRUCTURAL BIOLOGY, 1999, 6 (10) :932-936

← 1 2 3 4 →