Energetics of the cooperative assembly of cell division protein FtsZ and the nucleotide hydrolysis switch

被引:46
作者
Huecas, S [1 ]
Andreu, JM [1 ]
机构
[1] CSIC, Ctr Invest Biol, E-28040 Madrid, Spain
关键词
D O I
10.1074/jbc.M307128200
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
FtsZis the first protein recruited to the bacterial division site, where it forms the cytokinetic Z ring. We have determined the functional energetics of FtsZ assembly, employing FtsZ from the thermophilic Archaea Methanococcus jannaschii bound to GTP, GMPCPP, GDP, or GMPCP, under different solution conditions. FtsZ oligomerizes in a magnesium-insensitive manner. FtsZ cooperatively assembles with magnesium and GTP or GMPCPP into large polymers, following a nucleated condensation polymerization mechanism, under nucleotide hydrolyzing and non-hydrolyzing conditions. The effect of temperature on the critical concentration indicates polymer elongation with an apparent heat capacity change of -800 +/- 100 cal mol(-1) K-1 and positive enthalpy and entropy changes, compatible with axial hydrophobic contacts of each FtsZ in the polymer, and predicts optimal polymer stability near 75 degreesC. Assembly entails the binding of one medium affinity magnesium ion and the uptake of one proton per FtsZ. Interestingly, GDP- or GMPCP-liganded FtsZ cooperatively form helically curved polymers, with an elongation only 1-2 kcal mol(-1) more unfavorable than the straight polymers formed with nucleotide triphosphate, suggesting a physiological requirement for FtsZ polymerization inhibitors. This GTP hydrolysis switch should provide the basic properties for FtsZ polymer disassembly and its functional dynamics.
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页码:46146 / 46154
页数:9
相关论文
共 75 条
[41]   Escherichia coli FtsZ polymers contain mostly GTP and have a high nucleotide turnover [J].
Mingorance, J ;
Rueda, S ;
Gómez-Puertas, P ;
Valencia, A ;
Vicente, M .
MOLECULAR MICROBIOLOGY, 2001, 41 (01) :83-91
[42]  
MINTON AP, 1994, MODERN ANAL ULTRACEN, P81
[43]   Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations [J].
Mukherjee, A ;
Lutkenhaus, J .
JOURNAL OF BACTERIOLOGY, 1999, 181 (03) :823-832
[44]   GUANINE NUCLEOTIDE-DEPENDENT ASSEMBLY OF FTSZ INTO FILAMENTS [J].
MUKHERJEE, A ;
LUTKENHAUS, J .
JOURNAL OF BACTERIOLOGY, 1994, 176 (09) :2754-2758
[45]   ESCHERICHIA-COLI CELL-DIVISION PROTEIN FTSZ IS A GUANINE-NUCLEOTIDE BINDING-PROTEIN [J].
MUKHERJEE, A ;
DAI, K ;
LUTKENHAUS, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (03) :1053-1057
[46]   Dynamic assembly of FtsZ regulated by GTP hydrolysis [J].
Mukherjee, A ;
Lutkenhaus, J .
EMBO JOURNAL, 1998, 17 (02) :462-469
[47]   High-resolution model of the microtubule [J].
Nogales, E ;
Whittaker, M ;
Milligan, RA ;
Downing, KH .
CELL, 1999, 96 (01) :79-88
[48]   Structure of the αβtubulin dimer by electron crystallography [J].
Nogales, E ;
Wolf, SG ;
Downing, KH .
NATURE, 1998, 391 (6663) :199-203
[49]   Tubulin rings: which way do they curve? [J].
Nogales, E ;
Wang, HW ;
Niederstrasser, H .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2003, 13 (02) :256-261
[50]   Assembly of archaeal cell division protein FtsZ and a GTPase-inactive mutant into double-stranded filaments [J].
Oliva, MA ;
Huecas, S ;
Palacios, JM ;
Martín-Benito, J ;
Valpuesta, JM ;
Andreu, JM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (35) :33562-33570