BIOMAT Database Logo BIOMAT Database Logo

Both temperature and medium composition regulate RNase E processing efficiency of the rpsO mRNA coding for ribosomal protein S15 of Escherichia coli. 2002

J Le Derout, and P Régnier, and E Hajnsdorf
UPR 9073 du CNRS, Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France.

Cleavage by RNase E is believed to be the rate-limiting step in the degradation of many RNAs. These cleavages are modulated by 5' end-phosphorylation, folding and translation of the mRNA in question. Here, we present data suggesting that these cleavages are also regulated by environmental conditions. We report that rpsO mRNA, 15 minutes after a shift to 44 degrees C, is stabilized in cells grown in minimal medium. This stabilization is correlated with a reduction in the efficiency of the RNase E cleavage which initiates its decay. We also observe the appearance of RNA fragments previously detected following RNase E inactivation and a defect in the adaptation of RNase E concentration. These observations, coupled to the fact that RNase E overproduction slightly reduces the accumulation of the rpsO mRNA, suggest that this stabilization is caused in part by a limitation in RNase E concentration. An increase in the steady-state level of rpsT mRNA is also observed following a shift to 44 degrees C in minimal medium; however, processing of the 9 S rRNA precursor is not affected under these conditions. We thus propose that RNase E concentration changes in the cell in response to environmental conditions and that these changes can selectively affect the processing and the stability of individual mRNAs. Our data also indicate that the efficiency of cleavage of the rpsO mRNA by RNase E is modified by other factor(s) which remain to be identified.

UI MeSH Term Description Entries
D003470 Culture Media Any liquid or solid preparation made specifically for the growth, storage, or transport of microorganisms or other types of cells. The variety of media that exist allow for the culturing of specific microorganisms and cell types, such as differential media, selective media, test media, and defined media. Solid media consist of liquid media that have been solidified with an agent such as AGAR or GELATIN. Media, Culture
D004722 Endoribonucleases A family of enzymes that catalyze the endonucleolytic cleavage of RNA. It includes EC 3.1.26.-, EC 3.1.27.-, EC 3.1.30.-, and EC 3.1.31.-. Endoribonuclease
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D005798 Genes, Bacterial The functional hereditary units of BACTERIA. Bacterial Gene,Bacterial Genes,Gene, Bacterial
D012269 Ribosomal Proteins Proteins found in ribosomes. They are believed to have a catalytic function in reconstituting biologically active ribosomal subunits. Proteins, Ribosomal,Ribosomal Protein,Protein, Ribosomal
D012323 RNA Processing, Post-Transcriptional Post-transcriptional biological modification of messenger, transfer, or ribosomal RNAs or their precursors. It includes cleavage, methylation, thiolation, isopentenylation, pseudouridine formation, conformational changes, and association with ribosomal protein. Post-Transcriptional RNA Modification,RNA Processing,Post-Transcriptional RNA Processing,Posttranscriptional RNA Processing,RNA Processing, Post Transcriptional,RNA Processing, Posttranscriptional,Modification, Post-Transcriptional RNA,Modifications, Post-Transcriptional RNA,Post Transcriptional RNA Modification,Post Transcriptional RNA Processing,Post-Transcriptional RNA Modifications,Processing, Posttranscriptional RNA,Processing, RNA,RNA Modification, Post-Transcriptional,RNA Modifications, Post-Transcriptional
D012329 RNA, Bacterial Ribonucleic acid in bacteria having regulatory and catalytic roles as well as involvement in protein synthesis. Bacterial RNA
D012333 RNA, Messenger RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm. Messenger RNA,Messenger RNA, Polyadenylated,Poly(A) Tail,Poly(A)+ RNA,Poly(A)+ mRNA,RNA, Messenger, Polyadenylated,RNA, Polyadenylated,mRNA,mRNA, Non-Polyadenylated,mRNA, Polyadenylated,Non-Polyadenylated mRNA,Poly(A) RNA,Polyadenylated mRNA,Non Polyadenylated mRNA,Polyadenylated Messenger RNA,Polyadenylated RNA,RNA, Polyadenylated Messenger,mRNA, Non Polyadenylated
D012341 RNA, Ribosomal, 5S Constituent of the 50S subunit of prokaryotic ribosomes containing about 120 nucleotides and 34 proteins. It is also a constituent of the 60S subunit of eukaryotic ribosomes. 5S rRNA is involved in initiation of polypeptide synthesis. 5S Ribosomal RNA,5S rRNA,RNA, 5S Ribosomal,Ribosomal RNA, 5S,rRNA, 5S
D013696 Temperature The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms. Temperatures

Related Publications

J Le Derout, and P Régnier, and E Hajnsdorf
Cloning of rpsO, the gene for ribosomal protein S15 of Escherichia coli.
January 1982, Molecular & general genetics : MGG,
J Le Derout, and P Régnier, and E Hajnsdorf
Nucleotide sequence of the gene for Escherichia coli ribosomal protein S15 (rpsO).
January 1984, Molecular & general genetics : MGG,
J Le Derout, and P Régnier, and E Hajnsdorf
Specific recognition of rpsO mRNA and 16S rRNA by Escherichia coli ribosomal protein S15 relies on both mimicry and site differentiation.
May 2004, Molecular microbiology,
J Le Derout, and P Régnier, and E Hajnsdorf
A pseudoknot is required for efficient translational initiation and regulation of the Escherichia coli rpsO gene coding for ribosomal protein S15.
January 1995, Biochemistry and cell biology = Biochimie et biologie cellulaire,
J Le Derout, and P Régnier, and E Hajnsdorf
E. coli RpsO mRNA decay: RNase E processing at the beginning of the coding sequence stimulates poly(A)-dependent degradation of the mRNA.
March 1999, Journal of molecular biology,
J Le Derout, and P Régnier, and E Hajnsdorf
Initiation, attenuation and RNase III processing of transcripts from the Escherichia coli operon encoding ribosomal protein S15 and polynucleotide phosphorylase.
January 1986, Journal of molecular biology,
J Le Derout, and P Régnier, and E Hajnsdorf
Translational autocontrol of the Escherichia coli ribosomal protein S15.
January 1990, Journal of molecular biology,
J Le Derout, and P Régnier, and E Hajnsdorf
RNase E processing of essential cell division genes mRNA in Escherichia coli.
August 1996, Nucleic acids research,
J Le Derout, and P Régnier, and E Hajnsdorf
Uncovering a delicate balance between endonuclease RNase III and ribosomal protein S15 in E. coli ribosome assembly.
December 2021, Biochimie,
J Le Derout, and P Régnier, and E Hajnsdorf
Decay of mRNA encoding ribosomal protein S15 of Escherichia coli is initiated by an RNase E-dependent endonucleolytic cleavage that removes the 3' stabilizing stem and loop structure.
January 1991, Journal of molecular biology,
Copied contents to your clipboard!