Crystal Structures of Phd-Doc, HigA, and YeeU Establish Multiple Evolutionary Links between Microbial Growth-Regulating Toxin-Antitoxin Systems

被引：57

作者：

Arbing, Mark A. ^{[1
]}

Handelman, Samuel K. ^{[1
]}

Kuzin, Alexandre P. ^{[1
]}

Verdon, Gregory ^{[1
]}

Wang, Chi ^{[1
]}

Su, Min ^{[1
]}

Rothenbacher, Francesca P. ^{[3
]}

Abashidze, Mariam ^{[1
]}

Liu, Mohan ^{[3
]}

Hurley, Jennifer M. ^{[3
]}

Xiao, Rong ^{[4
,5
]}

Acton, Thomas ^{[4
,5
]}

Inouye, Masayori ^{[2
,4
,5
]}

Montelione, Gaetano T. ^{[4
,5
]}

Woychik, Nancy A. ^{[3
]}

Hunt, John F. ^{[1
]}

机构：

[1] Columbia Univ, Dept Biol Sci, New York, NY 10027 USA

[2] Univ Med & Dent New Jersey, Dept Biochem, Robert Wood Johnson Med Sch, Piscataway, NJ 08854 USA

[3] Univ Med & Dent New Jersey, Dept Mol Genet Microbiol & Immunol, Robert Wood Johnson Med Sch, Piscataway, NJ 08854 USA

[4] Rutgers State Univ, Ctr Adv Technol & Med, Piscataway, NJ 08854 USA

[5] Rutgers State Univ, Dept Mol Biol & Biochem, Piscataway, NJ 08854 USA

来源：

STRUCTURE | 2010年 / 18卷 / 08期

基金：

美国国家卫生研究院;

关键词：

MESSENGER-RNA INTERFERASE; ESCHERICHIA-COLI; CATALYTIC SITE; PROTEIN; DNA; P1; BINDING; ASSOCIATION; AMPYLATION; MECHANISM;

D O I：

10.1016/j.str.2010.04.018

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：

Bacterial toxin-antitoxin (TA) systems serve a variety of physiological functions including regulation of cell growth and maintenance of foreign genetic elements. Sequence analyses suggest that TA families are linked by complex evolutionary relationships reflecting likely swapping of functional domains between different TA families. Our crystal structures of Phd-Doc from bacteriophage P1, the HigA antitoxin from Escherichia coli CFT073, and YeeU of the YeeUWV systems from E. coli K12 and Shigella flexneri confirm this inference and reveal additional, unanticipated structural relationships. The growth-regulating Doc toxin exhibits structural similarity to secreted virulence factors that are toxic for eukaryotic target cells. The Phd antitoxin possesses the same fold as both the YefM and NE2111 antitoxins that inhibit structurally unrelated toxins. YeeU, which has an antitoxin-like activity that represses toxin expression, is structurally similar to the ribosome-interacting toxins YoeB and ReIE. These observations suggest extensive functional exchanges have occurred between TA systems during bacterial evolution.

引用

页码：996 / 1010

页数：15

共 62 条

[1] SPECIFICITY OF MINOR-GROOVE AND MAJOR-GROOVE INTERACTIONS IN A HOMEODOMAIN-DNA COMPLEX [J].

ADES, SE ;

SAUER, RT .

BIOCHEMISTRY, 1995, 34 (44) :14601-14608

[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] New connections in the prokaryotic toxin-antitoxin network: relationship with the eukaryotic nonsense-mediated RNA decay system [J].

Anantharaman, V ;

Aravind, L .

GENOME BIOLOGY, 2003, 4 (12)

[4] Evolution of protein fold in the presence of functional constraints [J].

Andreeva, Antonina ;

Murzin, Alexey G. .

CURRENT OPINION IN STRUCTURAL BIOLOGY, 2006, 16 (03) :399-408

[5] The 2.3-Å crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase [J].

Benach, J ;

Lee, I ;

Edstrom, W ;

Kuzin, AP ;

Chiang, YW ;

Acton, TB ;

Montelione, GT ;

Hunt, JF .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (21) :19176-19182

[6] The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit [J].

Brodersen, DE ;

Clemons, WM ;

Carter, AP ;

Morgan-Warren, RJ ;

Wimberly, BT ;

Ramakrishnan, V .

CELL, 2000, 103 (07) :1143-1154

[7] Three Dimensional Structure of the MqsR: MqsA Complex: A Novel TA Pair Comprised of a Toxin Homologous to RelE and an Antitoxin with Unique Properties [J].

Brown, Breann L. ;

Grigoriu, Simina ;

Kim, Younghoon ;

Arruda, Jennifer M. ;

Davenport, Andrew ;

Wood, Thomas K. ;

Peti, Wolfgang ;

Page, Rebecca .

PLOS PATHOGENS, 2009, 5 (12)

[8] A novel family of Eschefichia coli toxin-antitoxin gene pairs [J].

Brown, JM ;

Shaw, KJ .

JOURNAL OF BACTERIOLOGY, 2003, 185 (22) :6600-6608

[9] Crystallography & NMR system:: A new software suite for macromolecular structure determination [J].

Brunger, AT ;

Adams, PD ;

Clore, GM ;

DeLano, WL ;

Gros, P ;

Grosse-Kunstleve, RW ;

Jiang, JS ;

Kuszewski, J ;

Nilges, M ;

Pannu, NS ;

Read, RJ ;

Rice, LM ;

Simonson, T ;

Warren, GL .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1998, 54 :905-921

[10] RelE toxins from Bacteria and Archaea cleave mRNAs on translating ribosomes, which are rescued by tmRNA [J].

Christensen, SK ;

Gerdes, K .

MOLECULAR MICROBIOLOGY, 2003, 48 (05) :1389-1400

← 1 2 3 4 5 6 7 →