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The iscS gene deficiency affects the expression of pyrimidine metabolism genes.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2008 Aug 01; Vol. 372 (3), pp. 407-11. Date of Electronic Publication: 2008 May 13. - Publication Year :
- 2008
-
Abstract
- Inactivation of iscS encoding cysteine desulfurase results in a slow growth phenotype associated with the deficiency of iron-sulfur clusters, thiamine, NAD, and tRNA thionucleosides in Escherichia coli. However, the other roles of iscSin vivo are unknown. By using differential screening strategies, we identified 2 pyrimidine salvage enzymes, namely, uridine phosphorylase and cytidine deaminase, which were down-regulated in the iscS mutant. Both enzymes are positively regulated by the cAMP receptor protein (CRP). We also identified a novel protein complex, namely, YeiT-YeiA, whose expression level was decreased in the iscS mutant. The recombinant YeiT-YeiA complex exhibited NADH-dependent dihydropyrimidine dehydrogenase activity, indicating its role in pyrimidine metabolism. The presence of a CRP-binding consensus sequence on the 5'-upstream of the yeiT-YeiA gene suggests its regulation by CRP. These results provide a clue to the possible role of iscS in pyrimidine metabolism by gene regulation.
- Subjects :
- Base Sequence
Carbon-Sulfur Lyases genetics
Consensus Sequence
Cyclic AMP Receptor Protein metabolism
Cytidine Deaminase genetics
Cytidine Deaminase metabolism
Dihydrouracil Dehydrogenase (NAD+) genetics
Dihydrouracil Dehydrogenase (NAD+) metabolism
Dihydrouracil Dehydrogenase (NADP) metabolism
Down-Regulation
Electrophoresis, Gel, Two-Dimensional
Escherichia coli Proteins genetics
Escherichia coli Proteins metabolism
Mutation
Transcription Factors metabolism
Uridine Phosphorylase genetics
Uridine Phosphorylase metabolism
Carbon-Sulfur Lyases physiology
Escherichia coli genetics
Escherichia coli metabolism
Escherichia coli Proteins physiology
Gene Expression Regulation, Bacterial
Pyrimidines metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1090-2104
- Volume :
- 372
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 18482579
- Full Text :
- https://doi.org/10.1016/j.bbrc.2008.05.019