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The endoribonucleolytic N-terminal half of Escherichia coli RNase E is evolutionarily conserved in Synechocystis sp. and other bacteria but not the C-terminal half, which is sufficient for degradosome assembly.
- Source :
-
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 1998 Sep 29; Vol. 95 (20), pp. 11637-42. - Publication Year :
- 1998
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Abstract
- Escherichia coli RNase E, an essential single-stranded specific endoribonuclease, is required for both ribosomal RNA processing and the rapid degradation of mRNA. The availability of the complete sequences of a number of bacterial genomes prompted us to assess the evolutionarily conservation of bacterial RNase E. We show here that the sequence of the N-terminal endoribonucleolytic domain of RNase E is evolutionarily conserved in Synechocystis sp. and other bacteria. Furthermore, we demonstrate that the Synechocystis sp. homologue binds RNase E substrates and cleaves them at the same position as the E. coli enzyme. Taken together these results suggest that RNase E-mediated mechanisms of RNA decay are not confined to E. coli and its close relatives. We also show that the C-terminal half of E. coli RNase E is both sufficient and necessary for its physical interaction with the 3'-5' exoribonuclease polynucleotide phosphorylase, the RhlB helicase, and the glycolytic enzyme enolase, which are components of a "degradosome" complex. Interestingly, however, the sequence of the C-terminal half of E. coli RNase E is not highly conserved evolutionarily, suggesting diversity of RNase E interactions with other RNA decay components in different organisms. This notion is supported by our finding that the Synechocystis sp. RNase E homologue does not function as a platform for assembly of E. coli degradosome components.
- Subjects :
- Base Sequence
Conserved Sequence
DNA Primers genetics
Endoribonucleases chemistry
Endoribonucleases metabolism
Macromolecular Substances
RNA Processing, Post-Transcriptional
RNA, Bacterial metabolism
RNA, Messenger metabolism
RNA, Ribosomal metabolism
Species Specificity
Substrate Specificity
Cyanobacteria enzymology
Cyanobacteria genetics
Endoribonucleases genetics
Escherichia coli enzymology
Escherichia coli genetics
Evolution, Molecular
Subjects
Details
- Language :
- English
- ISSN :
- 0027-8424
- Volume :
- 95
- Issue :
- 20
- Database :
- MEDLINE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 9751718
- Full Text :
- https://doi.org/10.1073/pnas.95.20.11637