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PMID: 7732015 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Polyadenylylation destabilizes the rpsO mRNA of Escherichia coli.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 92 ·No. 9 ·1995-04-25 ·Pages 3973-7

Hajnsdorf E, Braun F, Haugel-Nielsen J, Régnier P

Abstract

The rpsO mRNA, encoding ribosomal protein S15, is only partly stabilized when the three ribonucleases implicated in its degradation--RNase E, polynucleotide phosphorylase, and RNase II--are inactivated. In the strain deficient for RNase E and 3'-to-5' exoribonucleases, degradation of this mRNA is correlated with the appearance of posttranscriptionally elongated molecules. We report that these elongated mRNAs harbor poly(A) tails, most of which are fused downstream of the 3'-terminal hairpin at the site where transcription terminates. Poly(A) tails are shorter in strains containing 3'-to-5' exoribonucleases. Inactivation of poly(A) polymerase I (pcnB) prevents polyadenylylation and stabilizes the rpsO mRNA if RNase E is inactive. In contrast polyadenylylation does not significantly modify the stability of rpsO mRNA undergoing RNase E-mediated degradation.

Related Genes
rpsO
MeSH Terms
Base Sequence Blotting, Northern DNA Primers Escherichia coli/genetics,metabolism Genes, Bacterial Kinetics Molecular Sequence Data Poly A/analysis Polymerase Chain Reaction RNA, Messenger/biosynthesis,chemistry Ribosomal Proteins/biosynthesis,genetics Time Factors
Chemicals
DNA Primers RNA, Messenger Ribosomal Proteins ribosomal protein S15 Poly A
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Hajnsdorf E
Institut de Biologie Physico-Chimique, Paris, France.
Braun F
Haugel-Nielsen J
Régnier P
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.92.9.3973
Published
1995-04-25
Pages
3973-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC42084
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.92.9.3973 PMC Full Text View journal details
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