Abstract |
A second secreted ribonuclease, designated binase II, has been detected in Bacillus intermedius 7P, and its structural gene was cloned and sequenced. Unlike the well-known binase I, a 109-amino acid guanyl-specific enzyme, the 292-residue binase II is closely related to the B. subtilis nuclease Bsn, in structure and in its enzymatic properties. Binase II is also insensitive to inactivation by barstar, an inhibitor protein that is specific for guanyl-specific ribonucleases. While both B. intermedius enzymes are induced upon phosphate starvation, only the gene for binase I belongs to the pho regulon system and carries pho-box elements adjacent to its promoter sequence. The gene for binase II is similar to that for Bsn in lacking such elements. The birB gene coding for binase II appears to be located next to the 3'-end of a ferric ion transport operon, with which it convergently overlaps. This would allow attenuator control over binase II expression under conditions of starvation for ferric ions.
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Authors | E Hahnen, L Znamenskaya, D Koczan, I Leshchinskaya, G Hobom |
Journal | Molecular & general genetics : MGG
(Mol Gen Genet)
Vol. 263
Issue 4
Pg. 571-80
(May 2000)
ISSN: 0026-8925 [Print] Germany |
PMID | 10852477
(Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- RNA, Messenger
- Recombinant Proteins
- Endoribonucleases
- ribonuclease T(2)
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Topics |
- Amino Acid Sequence
- Bacillus
(enzymology, genetics)
- Bacillus subtilis
(enzymology, genetics, growth & development)
- Base Sequence
- Cloning, Molecular
- Endoribonucleases
(genetics)
- Escherichia coli
- Gene Expression Regulation, Bacterial
- Gene Expression Regulation, Enzymologic
- Genes, Bacterial
- Genes, Reporter
- Genotype
- Kinetics
- Molecular Sequence Data
- Nucleic Acid Conformation
- Protein Biosynthesis
- RNA, Messenger
(chemistry, genetics)
- Recombinant Proteins
(chemistry, metabolism)
- Restriction Mapping
- Sequence Alignment
- Sequence Homology, Amino Acid
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