Assembly of an FtsZ mutant deficient in GTPase activity has implications for FtsZ assembly and the role of the Z ring in cell division

被引:65
作者
Mukherjee, A
Saez, C
Lutkenhaus, J
机构
[1] Univ Kansas, Med Ctr, Dept Microbiol Mol Genet & Immunol, Kansas City, KS 66160 USA
[2] Univ Missouri, Sch Biol Sci, Kansas City, MO 64110 USA
关键词
D O I
10.1128/JB.183.24.7190-7197.2001
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
FtsZ,. the ancestral homologue of eukaryotic tubulins, assembles into the Z ring, which is required for cytokinesis in prokaryotic cells. Both FtsZ and tubulin have a GTPase activity associated with polymerization. Interestingly, the ftsZ2 mutant is viable, although the FtsZ2 mutant protein has dramatically reduced GTPase activity due to a glycine-for-aspartic acid substitution within the synergy loop. In this study, we have examined Illyc the properties of FtsZ2 and found that the reduced GTPase activity is not enhanced by DEAE-dextran-induced assembly, indicating it has a defective catalytic site. In the absence of DEAE-dextran, FtsZ2 fails to assemble unless supplemented with wild-type FtsZ. FtsZ has to be at or above the critical concentration for copolymerization to occur, indicating that FtsZ is nucleating the copolymers. The copolymers formed are relatively stable and appear to be stabilized by a GTP-cap. These results indicate that FtsZ2 cannot nucleate assembly in vitro, although it must in vivo. Furthermore, the stability of FtsZ-FtsZ2 copolymers argues that FtsZ2 polymers would be stable, suggesting. that stable FtsZ polymers are able to support cell division.
引用
收藏
页码:7190 / 7197
页数:8
相关论文
共 42 条
[1]   SEDIMENTATION EQUILIBRIUM IN REACTING SYSTEMS .6. SOME APPLICATIONS TO INDEFINITE SELF-ASSOCIATIONS . STUDIES WITH BETA-LACTOGLOBULIN A [J].
ADAMS, ET ;
LEWIS, MS .
BIOCHEMISTRY, 1968, 7 (03) :1044-&
[2]   ANALYSIS OF FTSZ MUTATIONS THAT CONFER RESISTANCE TO THE CELL-DIVISION INHIBITOR SULA (SFIA) [J].
BI, E ;
LUTKENHAUS, J .
JOURNAL OF BACTERIOLOGY, 1990, 172 (10) :5602-5609
[3]   ISOLATION AND CHARACTERIZATION OF FTSZ ALLELES THAT AFFECT SEPTAL MORPHOLOGY [J].
BI, E ;
LUTKENHAUS, J .
JOURNAL OF BACTERIOLOGY, 1992, 174 (16) :5414-5423
[4]   CELL-DIVISION INHIBITORS SULA AND MINCD PREVENT FORMATION OF THE FTSZ RING [J].
BI, E ;
LUTKENHAUS, J .
JOURNAL OF BACTERIOLOGY, 1993, 175 (04) :1118-1125
[5]   FTSZ RING STRUCTURE ASSOCIATED WITH DIVISION IN ESCHERICHIA-COLI [J].
BI, E ;
LUTKENHAUS, J .
NATURE, 1991, 354 (6349) :161-164
[6]   Bacterial cell division [J].
Bramhill, D .
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, 1997, 13 :395-424
[7]   MUTATIONS IN FTSZ THAT CONFER RESISTANCE TO SULA AFFECT THE INTERACTION OF FTSZ WITH GTP [J].
DAI, K ;
MUKHERJEE, A ;
XU, YF ;
LUTKENHAUS, J .
JOURNAL OF BACTERIOLOGY, 1994, 176 (01) :130-136
[8]   THE ESSENTIAL BACTERIAL CELL-DIVISION PROTEIN FTSZ IS A GTPASE [J].
DEBOER, P ;
CROSSLEY, R ;
ROTHFIELD, L .
NATURE, 1992, 359 (6392) :254-256
[9]  
Durchschlag H., 1986, THERMODYNAMIC DATA B, P45, DOI 10.1007/978-3-642-71114-5_3
[10]   Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers [J].
Erickson, HP ;
Taylor, DW ;
Taylor, KA ;
Bramhill, D .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (01) :519-523