Abstract:
:The Escherichia coli HtrA protein is a periplasmic protease/chaperone that is upregulated under stress conditions. The protease and chaperone activities of HtrA eliminate or refold damaged and unfolded proteins in the bacterial periplasm that are generated upon stress conditions. In the absence of substrates, HtrA oligomerizes into a hexameric cage, but binding of misfolded proteins transforms the hexamers into bigger 12-mer and 24-mer cages that encapsulate the substrates for degradation or refolding. HtrA also undergoes partial degradation as a consequence of self-cleavage of the mature protein, producing short-HtrA protein (s-HtrA). The aim of this study was to examine the physiological role of this self-cleavage process. We found that the only requirement for self-cleavage of HtrA into s-HtrA in vitro was the hydrolysis of protein substrates. In fact, peptides resulting from the hydrolysis of the protein substrates were sufficient to induce autocleavage. However, the continuous presence of full-length substrate delayed the process. In addition, we observed that the hexameric cage structure is required for autocleavage and that s-HtrA accumulates only late in the degradation reaction. These results suggest that self-cleavage occurs when HtrA reassembles back into the resting hexameric structure and peptides resulting from substrate hydrolysis are allosterically stimulating the HtrA proteolytic activity. Our data support a model in which the physiological role of the self-cleavage process is to eliminate the excess of HtrA once the stress conditions cease.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Jomaa A,Iwanczyk J,Tran J,Ortega Jdoi
10.1128/JB.01187-08subject
Has Abstractpub_date
2009-03-01 00:00:00pages
1924-32issue
6eissn
0021-9193issn
1098-5530pii
JB.01187-08journal_volume
191pub_type
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journal_title:Journal of bacteriology
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doi:10.1128/jb.168.1.365-373.1986
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.109.1.196-202.1972
更新日期:1972-01-01 00:00:00
abstract::The gltA gene, encoding Sinorhizobium meliloti 104A14 citrate synthase, was isolated by complementing an Escherichia coli gltA mutant. The S. meliloti gltA gene was mutated by inserting a kanamycin resistance gene and then using homologous recombination to replace the wild-type gltA with the gltA::kan allele. The resu...
journal_title:Journal of bacteriology
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journal_title:Journal of bacteriology
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doi:10.1128/jb.167.3.935-939.1986
更新日期:1986-09-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:1965-03-01 00:00:00
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更新日期:1979-01-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:1986-03-01 00:00:00
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pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:1990-02-01 00:00:00
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journal_title:Journal of bacteriology
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doi:10.1128/JB.161.2.681-686.1985
更新日期:1985-02-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.83.1.97-99.1962
更新日期:1962-01-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/jb.174.22.7245-7252.1992
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更新日期:1979-11-01 00:00:00
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更新日期:1969-10-01 00:00:00
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更新日期:1986-09-01 00:00:00
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更新日期:1992-12-01 00:00:00
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journal_title:Journal of bacteriology
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更新日期:1973-09-01 00:00:00
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pub_type: 杂志文章
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更新日期:1982-01-01 00:00:00