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PMID:8969495
| Citation |
Scotti, C, Valbuzzi, A, Perego, M, Galizzi, A and Albertini, AM (1996) The Bacillus subtilis genes for ribonucleotide reductase are similar to the genes for the second class I NrdE/NrdF enzymes of Enterobacteriaceae. Microbiology (Reading, Engl.) 142 ( Pt 11):2995-3004 |
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| Abstract |
We have cloned and sequenced the nrd (nucleotide reductase) locus of Bacillus subtilis. The locus seems to be organized in an operon comprising four ORFs. The first three encode polypeptides highly similar to the product of the coding sequences characterizing the nrdEF operons of Enterobacteriaceae. The sequencing of the conditional lethal mutation ts-A13, localized in the nrdE cistron, and the lethality of insertional mutations targeted in the internal region of nrdE and nrdF, demonstrated the essential role of this locus. The fourth ORF, ymaB, part of the putative operon, which is not similar to any known protein, is also essential. The regulation of expression of the operon, monitored by lacZ transcriptional fusions, is similar to the regulation of the functionally relevant nrdAB operon of Escherichia coli. The operon was induced by thymidine starvation and its expression was directly or indirectly affected by RecA function. Genetic and functional analysis strongly indicates that in B. subtilis the class I ribonucleotide reductase encoded by this nrd operon is evolutionarily distant from the homologous class I enzyme of Enterobacteria. |
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| Keywords |
Amino Acid Sequence; Bacillus subtilis/enzymology; Bacillus subtilis/genetics; Base Sequence; Chromosome Mapping; Cloning, Molecular; DNA Primers/genetics; Enterobacteriaceae/enzymology; Enterobacteriaceae/genetics; Escherichia coli/genetics; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Genes, Bacterial; Molecular Sequence Data; Mutation; Open Reading Frames; Operon; Phylogeny; Ribonucleotide Reductases/classification; Ribonucleotide Reductases/genetics; Sequence Homology, Amino Acid; Species Specificity |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004748: ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
ECO:0000315: |
F |
This paper follows the studies in another article (PMID 4627024) which I don't have access to read past the beginning results and the abstract. This previous article used a temperature sensitive mutant ts-167 to determine the function of the nrdEF locus. That paper determined the function by analyzing the pool of dNTP present at the restrictive temperature. dCTP and dATP were not apparent at these restrictive temperatures. The reference listed above (PMID 8969495) used phylogeny and sequencing to determine that Enterobacteria favor the use of nrdAB loci, whereas Bacilus subtils has evolved to use nrdEF. They also used clone pMP25.8 to rescue the temperature sensitive mutant, and later sequenced the nrdE mutant to determine there were 2 neutral mutations and 1 mutation that led to the lethality of the temperature sensitive mutant. They concluded that this mutation was the cause for the loss of function of the NrdE protein. The mutant lethality due to the loss of dCTP and dATP synthesis provides evidenct that this gene is responsible for the essential enzyme responsible for reductase activity for the respective ribonucleoside-diphosphates. |
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