Straight and curved conformations of FtsZ are regulated by GTP hydrolysis

被引:235
作者
Lu, CL [1 ]
Reedy, M [1 ]
Erickson, HP [1 ]
机构
[1] Duke Univ, Med Ctr, Dept Cell Biol, Durham, NC 27710 USA
关键词
D O I
10.1128/JB.182.1.164-170.2000
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
FtsZ assembles in vitro into protofilaments that can adopt two conformations-the straight conformation, which can assemble further into two-dimensional protofilament sheets, and the curved conformation, which forms minirings about 23 nm in diameter. Here, we describe the structure of FtsZ tubes, which are a variation of the curved conformation. In the tube the curved protofilament forms a shallow helix with a diameter of 23 nm and a pitch of 18 or 24 degrees, We suggest that this shallow helix is the relaxed structure of the curved protofilament in solution. We provide evidence that GTP favors the straight conformation while GDP favors the curved conformation. In particular, exclusively straight protofilaments and protofilament sheets are assembled in GMPCPP, a nonhydrolyzable GTP analog, or in GTP following chelation of Mg, which blocks GTP hydrolysis. Assembly in GDP produces exclusively tubes, The transition from straight protofilaments to the curved conformation may provide a mechanism whereby the energy of GTP hydrolysis is used to generate force for the constriction of the FtsZ ring in cell division.
引用
收藏
页码:164 / 170
页数:7
相关论文
共 28 条
[1]   FtsZ-spirals and -arcs determine the shape of the invaginating septa in some mutants of Escherichia coli [J].
Addinall, SG ;
Lutkenhaus, J .
MOLECULAR MICROBIOLOGY, 1996, 22 (02) :231-237
[2]   FtsZ ring formation in fts mutants [J].
Addinall, SG ;
Bi, EF ;
Lutkenhaus, J .
JOURNAL OF BACTERIOLOGY, 1996, 178 (13) :3877-3884
[3]   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
[4]   Bacterial cell division [J].
Bramhill, D .
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, 1997, 13 :395-424
[5]   THE FREE-ENERGY FOR HYDROLYSIS OF A MICROTUBULE-BOUND NUCLEOTIDE TRIPHOSPHATE IS NEAR ZERO - ALL OF THE FREE-ENERGY FOR HYDROLYSIS IS STORED IN THE MICROTUBULE LATTICE [J].
CAPLOW, M ;
RUHLEN, RL ;
SHANKS, J .
JOURNAL OF CELL BIOLOGY, 1994, 127 (03) :779-788
[6]   THE PROPER RATIO OF FTSZ TO FTSA IS REQUIRED FOR CELL-DIVISION TO OCCUR IN ESCHERICHIA-COLI [J].
DAI, K ;
LUTKENHAUS, J .
JOURNAL OF BACTERIOLOGY, 1992, 174 (19) :6145-6151
[7]   THE ESSENTIAL BACTERIAL CELL-DIVISION PROTEIN FTSZ IS A GTPASE [J].
DEBOER, P ;
CROSSLEY, R ;
ROTHFIELD, L .
NATURE, 1992, 359 (6392) :254-256
[8]   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
[9]   Atomic structures of tubulin and FtsZ [J].
Erickson, HP .
TRENDS IN CELL BIOLOGY, 1998, 8 (04) :133-137
[10]   FTSZ, A PROKARYOTIC HOMOLOG OF TUBULIN [J].
ERICKSON, HP .
CELL, 1995, 80 (03) :367-370