Document Detail


Increased expression of Escherichia coli polynucleotide phosphorylase at low temperatures is linked to a decrease in the efficiency of autocontrol.
MedLine Citation:
PMID:  11395447     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Polynucleotide phosphorylase (PNPase) synthesis is translationally autocontrolled via an RNase III-dependent mechanism, which results in a tight correlation between protein level and messenger stability. In cells grown at 18 degrees C, the amount of PNPase is twice that found in cells grown at 30 degrees C. To investigate whether this effect was transcriptional or posttranscriptional, the expression of a set of pnp-lacZ transcriptional and translational fusions was analyzed in cells grown at different temperatures. In the absence of PNPase, there was no increase in pnp-lacZ expression, indicating that the increase in pnp expression occurs at a posttranscriptional level. Other experiments clearly show that increased pnp expression at low temperature is only observed under conditions in which the autocontrol mechanism of PNPase is functional. At low temperature, the destabilizing effect of PNPase on its own mRNA is less efficient, leading to a decrease in repression and an increase in the expression level.
Authors:
N Mathy; A C Jarrige; M Robert-Le Meur; C Portier
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of bacteriology     Volume:  183     ISSN:  0021-9193     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2001 Jul 
Date Detail:
Created Date:  2001-06-07     Completed Date:  2001-07-12     Revised Date:  2013-04-17    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3848-54     Citation Subset:  IM    
Affiliation:
UPR9073 du CNRS, Institut de Biologie PhysicoChimique, 75005 Paris, France.
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MeSH Terms
Descriptor/Qualifier:
Cold Temperature
Endoribonucleases / metabolism
Escherichia coli / enzymology,  genetics*
Escherichia coli Proteins*
Gene Expression Regulation, Bacterial
Gene Expression Regulation, Enzymologic
Genes, Reporter
Lac Operon
Polyribonucleotide Nucleotidyltransferase / biosynthesis,  genetics*
Protein Biosynthesis
RNA Stability
Recombinant Fusion Proteins / biosynthesis
Ribonuclease III
Chemical
Reg. No./Substance:
0/Escherichia coli Proteins; 0/Recombinant Fusion Proteins; EC 2.7.7.8/Polyribonucleotide Nucleotidyltransferase; EC 3.1.-/Endoribonucleases; EC 3.1.26.3/Ribonuclease III; EC 3.1.26.3/ribonuclease III, E coli
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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