Cellular Localization of High-Molecular-Mass Heat Shock Proteins in Murine Cells

1994 ◽  
Vol 200 (3) ◽  
pp. 1367-1373 ◽  
Author(s):  
T. Hatayama ◽  
E. Nishiyama ◽  
K. Yasuda
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Mass ◽  
Cellular Localization ◽  
High Molecular Mass ◽  
Shock Proteins

scholarly journals Cloning and Expression of Murine High Molecular Mass Heat Shock Proteins, HSP105

1995 ◽  
Vol 270 (50) ◽  
pp. 29718-29723 ◽  
Author(s):  
Kunihiko Yasuda ◽  
Akira Nakai ◽  
Takumi Hatayama ◽  
Kazuhiro Nagata
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Mass ◽  
High Molecular Mass ◽  
Cloning And Expression ◽  
Shock Proteins

pH-induced changes of the structure of small heat shock proteins with molecular mass 24/27kDa (HspB1)

2004 ◽  
Vol 324 (4) ◽  
pp. 1199-1203 ◽  
Author(s):  
Ivan S. Chernik ◽  
Olesya O. Panasenko ◽  
Yi Li ◽  
Steven B. Marston ◽  
Nikolai B. Gusev
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Mass ◽  
Small Heat Shock Proteins ◽  
Shock Proteins ◽  
Induced Changes

Identification of mRNAs encoding low molecular mass heat-shock proteins in maize (Zea mays L.)

1986 ◽  
Vol 28 (6) ◽  
pp. 1106-1114 ◽  
Author(s):  
C. A. B. Rees ◽  
N. C. Hogan ◽  
D. B. Walden ◽  
B. G. Atkinson
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Mass ◽  
Polyclonal Antibodies ◽  
Relative Molecular Mass ◽  
Temperature Heat ◽  
Free Translation ◽  
Shock Proteins

Subjecting 5-day-old maize seedlings to a rapid elevation in growth temperature (heat shock; 25–42 °C) results in a shift in the pattern of protein synthesis in maize plumules from the production of a broad spectrum of proteins to the new and (or) enhanced synthesis of a small number of heat-shock proteins (HSPs). The low relative molecular mass (Mr) HSPs, and more specifically an 18-kDa HSP with four major isoelectric variants, represent the majority of HSP synthesis following cell-free translation of total cellular poly (A)+ RNAs and polyribosomal RNAs extracted from heat-shocked plumules. Immunochemical studies, using polyclonal antibodies raised against the 18-kDa HSPs, show that the 18-kDa HSPs synthesized in vitro share immunochemical properties with HSPs of the same Mr synthesized in vivo by heat-shocked plumules. Furthermore, size fractionation and translation analyses of total cellular poly(A)+ RNAs extracted from heat-shocked plumules demonstrate that poly(A)+ RNAs encoding an 18-kDa HSP(s) have an estimated size of 0.6–0.95 kilobases. The observation that 18-kDa HSPs are absent among the translation products and immunoprecipitates of proteins synthesized in vitro by RNAs extracted from control plumules (25 °C) suggests that the mRNAs encoding 18-kDa HSPs are heat-shock induced.Key words: mRNA, maize, heat shock.

Genetic regulation during heat shock and function of heat-shock proteins: a review

1983 ◽  
Vol 61 (6) ◽  
pp. 387-394 ◽  
Author(s):  
R. M. Tanguay
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Posttranscriptional Regulation ◽  
Translational Regulation ◽  
Cellular Localization ◽  
Molecular Mechanisms ◽  
Genetic Regulation ◽  
Protective Function ◽  
Shock Proteins ◽  
And Function

The induction by thermal stress of certain specific genes (heat-shock genes) first described in Drosophila has recently been observed in a wide variety of unicellular and multicellular organisms, emphasizing the basic importance of this ubiquitous response. Recent data dealing with the molecular mechanisms involved in the intensive transcriptional and posttranscriptional regulation during heat shock is reviewed with emphasis on the induction of the response and the putative function of the heat-shock proteins. A model showing the various interactions of cellular regulatory mechanisms operating in the heat-shocked cell is presented. While the list of agents or treatments inducing heat-shock proteins (hsp's) in various organisms is increasing, the identification of a hypothetical common inducing factor is elusive. The recently described reorganization of some cytoskeletal elements upon heat shock is discussed both in terms of its potential involvement in transcriptional and (or) translational regulation and of its putative relation with the cellular localization of the hsp's. Studies on the cellular localization of hsp's in various organisms do not show a clear uniform pattern which could help in elucidating the function of hsp's. On the other hand, studies on the thermal resistance of various cells types show a strong correlation between the induction of hsp's and the development of transitory thermotolerance. Such a protective function for hsp's can probably be extended to other types of cellular aggression.

scholarly journals The molecular evolution of the small heat-shock proteins in plants.

Genetics ◽  
1995 ◽  
Vol 141 (2) ◽  
pp. 785-795 ◽  
Author(s):  
E R Waters
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Cellular Localization ◽  
Higher Plants ◽  
Small Heat Shock Protein ◽  
Gene Families ◽  
Small Heat Shock Proteins ◽  
Amino Acid Sequences ◽  
Shock Proteins

Abstract The small heat-shock proteins have undergone a tremendous diversification in plants; whereas only a single small heat-shock protein is found in fungi and many animals, over 20 different small heat-shock proteins are found in higher plants. The small heat-shock proteins in plants have diversified in both sequence and cellular localization and are encoded by at least five gene families. In the study, 44 small heat-shock protein DNA and amino acid sequences were examined, using both phylogenetic analysis and analysis of nucleotide substitution patterns to elucidate the evolutionary history of the small heat-shock proteins. The phylogenetic relationships of the small heat-shock proteins, estimated using parsimony and distance methods, reveal the gene duplication, sequence divergence and gene conversion have all played a role in the evolution of the small heat-shock proteins. Analysis of nonsynonymous substitutions and conservative and radical replacement substitutions )in relation to hydrophobicity) indicates that the small heat-shock protein gene families are evolving at different rates. This suggests that the small heat-shock proteins may have diversified in function as well as in sequence and cellular localization.

scholarly journals Expression profiles of low molecular mass heat shock proteins byMycobacterium aviumandMycobacterium intracellulare

2001 ◽  
Vol 200 (2) ◽  
pp. 131-136 ◽  
Author(s):  
Haruaki Tomioka ◽  
Toshiaki Shimizu ◽  
Hiroko Kajitani ◽  
Katsumasa Sato ◽  
Chiaki Sano
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Mass ◽  
Expression Profiles ◽  
Shock Proteins
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