A natural osmolyte trimethylamine N-oxide promotes assembly and bundling of the bacterial cell division protein, FtsZ and counteracts the denaturing effects of urea

被引:37
作者
Mukherjee, A [1 ]
Santra, MK [1 ]
Beuria, TK [1 ]
Panda, D [1 ]
机构
[1] Indian Inst Technol, Sch Biosci & Bioengn, Bombay 400076, Maharashtra, India
关键词
FtsZ; FtsZ unfolding; osmolyte; protofilaments bundling; TMAO;
D O I
10.1111/j.1742-4658.2005.04696.x
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
Assembly of FtsZ was completely inhibited by low concentrations of urea and its unfolding occurred in two steps in the presence of urea, with the formation of an intermediate [Santra MK & Panda D (2003) J Biol Chem278, 21336-21343]. In this study, using the fluorescence of 1-anilininonaphthalene-8-sulfonic acid and far-UV circular dichroism spectroscopy, we found that a natural osmolyte, trimethylamine N-oxide (TMAO), counteracted the denaturing effects of urea and guanidium chloride on FtsZ. TMAO also protected assembly and bundling of FtsZ protofilaments from the denaturing effects of urea and guanidium chloride. Furthermore, the standard free energy changes for unfolding of FtsZ were estimated to be 22.5 and 28.4 kJ.mol(-1) in the absence and presence of 0.6 m TMAO, respectively. The data are consistent with the view that osmolytes counteract denaturant-induced unfolding of proteins by destabilizing the unfolded states. Interestingly, TMAO was also found to affect the assembly properties of native FtsZ. TMAO increased the light-scattering signal of the FtsZ assembly, increased sedimentable polymer mass, enhanced bundling of FtsZ protofilaments and reduced the GTPase activity of FtsZ. Similar to TMAO, monosodium glutamate, a physiological osmolyte in bacteria, which induces assembly and bundling of FtsZ filaments in vitro[Beuria TK, Krishnakumar SS, Sahar S, Singh N, Gupta K, Meshram M & Panda D (2003) J Biol Chem278, 3735-3741], was also found to counteract the deleterious effects of urea on FtsZ. The results together suggested that physiological osmolytes may regulate assembly and bundling of FtsZ in bacteria and that they may protect the functionality of FtsZ under environmental stress conditions.
引用
收藏
页码:2760 / 2772
页数:13
相关论文
共 66 条
[1]   Reversible unfolding of FtsZ cell division proteins from archaea and bacteria [J].
Andreu, JM ;
Oliva, MA ;
Monasterio, O .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (45) :43262-43270
[2]  
ARAKAWA T, 1984, J BIOL CHEM, V259, P4979
[3]   Jaws: The inside story. The metabolism of elasmobranch fishes [J].
Ballantyne, JS .
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, 1997, 118 (04) :703-742
[4]   Glutamate-induced assembly of bacterial cell division protein FtsZ [J].
Beuria, TK ;
Krishnakumar, SS ;
Sahar, S ;
Singh, N ;
Gupta, K ;
Meshram, M ;
Panda, D .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (06) :3735-3741
[5]  
BEVINTON PR, 1969, DATA REDUCTION ERROR
[6]  
Bolen D W, 2001, Methods Mol Biol, V168, P17
[7]   The osmophobic effect: Natural selection of a thermodynamic force in protein folding [J].
Bolen, DW ;
Baskakov, IV .
JOURNAL OF MOLECULAR BIOLOGY, 2001, 310 (05) :955-963
[8]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[9]   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
[10]   THE ESSENTIAL BACTERIAL CELL-DIVISION PROTEIN FTSZ IS A GTPASE [J].
DEBOER, P ;
CROSSLEY, R ;
ROTHFIELD, L .
NATURE, 1992, 359 (6392) :254-256