Neutron scattering: a tool to detect in vivo thermal stress effects at the molecular dynamics level in micro-organisms

被引:23
作者
Marty, Vincent [1 ,2 ]
Jasnin, Marion [3 ]
Fabiani, Elisa [2 ]
Vauclare, Pierre [1 ]
Gabel, Frank [4 ]
Trapp, Marcus [2 ,3 ]
Peters, Judith [2 ,3 ]
Zaccai, Giuseppe [1 ,3 ]
Franzetti, Bruno [1 ]
机构
[1] CNRS, Inst Biol Struct, F-38027 Grenoble, France
[2] Univ Grenoble 1, Inst Biol Struct, F-38000 Grenoble, France
[3] Inst Max Von Laue Paul Langevin, F-38042 Grenoble 9, France
[4] CEA, Inst Biol Struct, F-38054 Grenoble, France
关键词
protein folding; stress response; cell biology; MACROMOLECULAR DYNAMICS; PROTEIN; ADAPTATION; TRANSITION; MOTIONS;
D O I
10.1098/rsif.2013.0003
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
In vivo molecular dynamics in Halobacterium salinarum cells under stress conditions was measured by neutron scattering experiments coupled with microbiological characterization. Molecular dynamics alterations were detected with respect to unstressed cells, reflecting a softening of protein structures consistent with denaturation. The experiments indicated that the neutron scattering method provides a promising tool to study molecular dynamics modifications in the proteome of living cells induced by factors altering protein folds.
引用
收藏
页数:6
相关论文
共 23 条
[1]   Protein flexibility from the dynamical transition: A force constant analysis [J].
Bicout, DJ ;
Zaccai, G .
BIOPHYSICAL JOURNAL, 2001, 80 (03) :1115-1123
[2]   Stress regulation of the PAN-proteasome system in the extreme halophilic archaeon Halobacterium [J].
Chamieh, H. ;
Marty, V. ;
Guetta, D. ;
Perollier, A. ;
Franzetti, B. .
EXTREMOPHILES, 2012, 16 (02) :215-225
[3]   The two PAN ATPases from Halobacterium display N-terminal heterogeneity and form labile complexes with the 20S proteasome [J].
Chamieh, Hala ;
Guetta, Dorian ;
Franzetti, Bruno .
BIOCHEMICAL JOURNAL, 2008, 411 :387-397
[4]   Effects of Molecular Crowding on the Dynamics of Intrinsically Disordered Proteins [J].
Cino, Elio A. ;
Karttunen, Mikko ;
Choy, Wing-Yiu .
PLOS ONE, 2012, 7 (11)
[5]   Dynamics of apomyoglobin in the α-to-β transition and of partially unfolded aggregated protein [J].
Fabiani, E. ;
Stadler, A. M. ;
Madern, D. ;
Koza, M. M. ;
Tehei, M. ;
Hirai, M. ;
Zaccai, G. .
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 2009, 38 (02) :237-244
[6]  
GINZBURG M, 1970, Journal of General Physiology, V55, P187, DOI 10.1085/jgp.55.2.187
[7]   In vivo measurement of internal and global macromolecular motions in Escherichia coli [J].
Jasnin, M. ;
Moulin, M. ;
Haertlein, M. ;
Zaccai, G. ;
Tehei, M. .
BIOPHYSICAL JOURNAL, 2008, 95 (02) :857-864
[8]   Understanding the adaptation of Halobacterium species NRC-1 to its extreme environment through computational analysis of its genome sequence [J].
Kennedy, SP ;
Ng, WV ;
Salzberg, SL ;
Hood, L ;
DasSarma, S .
GENOME RESEARCH, 2001, 11 (10) :1641-1650
[9]   The thermosome: archetype of group II chaperonins [J].
Klumpp, M ;
Baumeister, W .
FEBS LETTERS, 1998, 430 (1-2) :73-77
[10]   Temperature-dependent structural and functional features of a hyperthermostable enzyme using elastic neutron scattering [J].
Koutsopoulos, S ;
van der Oost, J ;
Norde, W .
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2005, 61 (02) :377-384