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פותח על ידי קלירמאש פתרונות בע"מ -
Proteome analysis in the study of the bacterial heat-shock response
Year:
2002
Source of publication :
Mass Spectrometry Reviews
Authors :
רוזן, רן
;
.
Volume :
21
Co-Authors:
Rosen, R., Dept. Molec. Microbiol. Biotechnol., Tel Aviv University, Ramat Aviv, Tel Aviv 69978, Israel
Ron, E.Z., Dept. Molec. Microbiol. Biotechnol., Tel Aviv University, Ramat Aviv, Tel Aviv 69978, Israel
Facilitators :
From page:
244
To page:
265
(
Total pages:
22
)
Abstract:
In recent years, it has become clear that, in addition to the regulation of the expression of specific genes, there are global regulatory systems that control the simultaneous expression of a large number of genes in response to a variety of environmental stresses. The first of these global control systems, and of sub-stantial importance, is the heat-shock response. The heat-shock response is characterized by the induction of a large set of proteins (heat-shock proteins-HSPs) upon shifts to higher temperature and upon exposure to conditions in which proteins are denatured (i.e., alcohols, heavy metals). The heat-shock response is universal and many of the heat-shock proteins are highly conserved among species. In bacteria, the heat-shock response has been studied extensively in several Gram-positive bacteria (Bacillus subtilis) and in the Gram-negative bacteria (i.e., Escherichia coli, Agrobacterium tumefaciens). The first recognition of the molecular abundance of the bacterial heat-shock proteins look place with the introduction of high-resolution two-dimensional polyacrylamide gels (2D gels) to analyze complex mixtures of cellular proteins. Two-dimensional gels, followed by mass spectrometry, were used to define the heat-shock stimulons in several bacteria, and to study the regulatory elements that control the heat-shock response. Here, we review the heat-shock response and its regulation in bacteria. The review will emphasize The use ofproteome analysis in the study of this response, and will point out those open questions that can be investigated with proteomics, including mass spectrometry techniques.
Note:
Related Files :
bacteria
genetic engineering
Genetics
metabolism
proteins
temperature
עוד תגיות
תוכן קשור
More details
DOI :
10.1002/mas.10031
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
29900
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:50
Scientific Publication
Proteome analysis in the study of the bacterial heat-shock response
21
Rosen, R., Dept. Molec. Microbiol. Biotechnol., Tel Aviv University, Ramat Aviv, Tel Aviv 69978, Israel
Ron, E.Z., Dept. Molec. Microbiol. Biotechnol., Tel Aviv University, Ramat Aviv, Tel Aviv 69978, Israel
Proteome analysis in the study of the bacterial heat-shock response
In recent years, it has become clear that, in addition to the regulation of the expression of specific genes, there are global regulatory systems that control the simultaneous expression of a large number of genes in response to a variety of environmental stresses. The first of these global control systems, and of sub-stantial importance, is the heat-shock response. The heat-shock response is characterized by the induction of a large set of proteins (heat-shock proteins-HSPs) upon shifts to higher temperature and upon exposure to conditions in which proteins are denatured (i.e., alcohols, heavy metals). The heat-shock response is universal and many of the heat-shock proteins are highly conserved among species. In bacteria, the heat-shock response has been studied extensively in several Gram-positive bacteria (Bacillus subtilis) and in the Gram-negative bacteria (i.e., Escherichia coli, Agrobacterium tumefaciens). The first recognition of the molecular abundance of the bacterial heat-shock proteins look place with the introduction of high-resolution two-dimensional polyacrylamide gels (2D gels) to analyze complex mixtures of cellular proteins. Two-dimensional gels, followed by mass spectrometry, were used to define the heat-shock stimulons in several bacteria, and to study the regulatory elements that control the heat-shock response. Here, we review the heat-shock response and its regulation in bacteria. The review will emphasize The use ofproteome analysis in the study of this response, and will point out those open questions that can be investigated with proteomics, including mass spectrometry techniques.
Scientific Publication
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