Slow polymerization of Mycobacterium tuberculosis FtsZ

被引：110

作者：

White, EL ^{[1
]}

Ross, LJ ^{[1
]}

Reynolds, RC ^{[1
]}

Seitz, LE ^{[1
]}

Moore, GD ^{[1
]}

Borhani, DW ^{[1
]}

机构：

[1] So Res Inst, Dept Biochem & Mol Biol, Drug Discovery Div, Birmingham, AL 35205 USA

来源：

JOURNAL OF BACTERIOLOGY | 2000年 / 182卷 / 14期

关键词：

D O I：

10.1128/JB.182.14.4028-4034.2000

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The essential cell division protein. FtsZ, from Mycobacterium tuberculosis has been expressed in Escherichia coli and purified. The recombinant protein has GTPase activity typical of tubulin and other FtsZs. FtsZ polymerization was studied using 90 degrees light scattering. The mycobacterial protein reaches maximum polymerization much more slowly (similar to 10 min) than E. coli FtsZ. Depolymerization also occurs slowly, taking 1 h or longer under most conditions. Polymerization requires both Mg2+ and GTP, The minimum concentration of FtsZ needed for polymerization is 3 mu M. Electron microscopy shows that polymerized M. tuberculosis FtsZ consists of strands that associate to form ordered aggregates of parallel protofilaments. Ethyl 6-amino-2,3-dihydro-4-phenyl-1H-pyrido [4,3-b] [1,4] diazepin-8-ylcarbamate (SRI 7614), an inhibitor of tubulin polymerization synthesized at Southern Research Institute, inhibits M. tuberculosis FtsZ polymerization, inhibits GTP hydrolysis, and reduces the number and sizes of FtsZ polymers.

引用

页码：4028 / 4034

页数：7

共 33 条

[1] FTSZ RING STRUCTURE ASSOCIATED WITH DIVISION IN ESCHERICHIA-COLI [J].

BI, E ;

LUTKENHAUS, J .

NATURE, 1991, 354 (6349) :161-164

[2]

BOWDON BJ, 1987, CANCER RES, V47, P1621

[3]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[4] GTP-DEPENDENT POLYMERIZATION OF ESCHERICHIA-COLI FTSZ PROTEIN TO FORM TUBULES [J].

BRAMHILL, D ;

THOMPSON, CM .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (13) :5813-5817

[5] Microplate Alamar blue assay versus BACTEC 460 system for high-throughput screening of compounds against Mycobacterium tuberculosis and Mycobacterium avium [J].

Collins, LA ;

Franzblau, SG .

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 1997, 41 (05) :1004-1009

[6] THE ESSENTIAL BACTERIAL CELL-DIVISION PROTEIN FTSZ IS A GTPASE [J].

DEBOER, P ;

CROSSLEY, R ;

ROTHFIELD, L .

NATURE, 1992, 359 (6392) :254-256

[7] Tubulin secondary structure analysis, limited proteolysis sites, and homology to FtsZ [J].

dePereda, JM ;

Leynadier, D ;

Evangelio, JA ;

Chacon, P ;

Andreu, JM .

BIOCHEMISTRY, 1996, 35 (45) :14203-14215

[8]

ELLIS KJ, 1982, METHOD ENZYMOL, V87, P405

[9] Protofilaments and rings, two conformations of the tubulin family conserved from bacterial FtsZ to alpha/beta and gamma tubulin [J].

Erickson, HP ;

Stoffler, D .

JOURNAL OF CELL BIOLOGY, 1996, 135 (01) :5-8

[10] FTSZ, A PROKARYOTIC HOMOLOG OF TUBULIN [J].

ERICKSON, HP .

CELL, 1995, 80 (03) :367-370

← 1 2 3 4 →