Abstract |
Escherichia coli ribonucleases (RNases) HII, III, II, PH and D have been used to characterise new and known viral, bacterial, archaeal and eucaryotic sequences similar to these endo- (HII and III) and exoribonucleases (II, PH and D). Statistical models, hidden Markov models (HMMs), were created for the RNase HII, III, II and PH and D families as well as a double-stranded RNA binding domain present in RNase III. Results suggest that the RNase D family, which includes Werner syndrome protein and the 100 kDa antigenic component of the human polymyositis scleroderma (PMSCL) autoantigen, is a 3'-->5' exoribonuclease structurally and functionally related to the 3'-->5' exodeoxyribonuclease domain of DNA polymerases. Polynucleotide phosphorylases and the RNase PH family, which includes the 75 kDa PMSCL autoantigen, possess a common domain suggesting similar structures and mechanisms of action for these 3'-->5' phosphorolytic enzymes. Examination of HMM-generated multiple sequences alignments for each family suggest amino acids that may be important for their structure, substrate binding and/or catalysis.
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Authors | I S Mian |
Journal | Nucleic acids research
(Nucleic Acids Res)
Vol. 25
Issue 16
Pg. 3187-95
(Aug 15 1997)
ISSN: 0305-1048 [Print] England |
PMID | 9241229
(Publication Type: Comparative Study, Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, U.S. Gov't, P.H.S.)
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Chemical References |
- Escherichia coli Proteins
- RNA-Binding Proteins
- ribonuclease PH
- Endoribonucleases
- Exoribonucleases
- exoribonuclease II
- ribonuclease HII
- Ribonuclease III
- ribonuclease III, E coli
- Ribonuclease H
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Topics |
- Amino Acid Sequence
- Endoribonucleases
(genetics)
- Escherichia coli
(enzymology, genetics)
- Escherichia coli Proteins
- Exoribonucleases
(genetics)
- Genes, Bacterial
- Genes, Fungal
- Humans
- Molecular Sequence Data
- RNA-Binding Proteins
(genetics)
- Ribonuclease H
(genetics)
- Ribonuclease III
- Sequence Alignment
- Sequence Analysis
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