Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.30.1 (S1 nuclease)
 3,660 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The Na, K-ATPase is formed by two major subunits (alpha and beta) encoded by a gene family of at least four alpha and three beta isoforms. These genes show distinctive expression patterns involving complex tissue-specific and developmental regulation, although the control mechanisms are not well understood. Here we study the role of chromatin structure in the tissue-specific expression of rat Na, K-ATPase beta2 isoform, which is mainly found in the central nervous system. We have examined the presence and characteristics of nuclease hypersensitive sites and the cytosine methylation patterns in the 5'-flanking region of the beta2 isoform gene from various nuclear preparations. Our results show that in this 5'-flanking region there is only one nuclease hypersensitive site. It is located upstream of the transcription initiation site and shows tissue-specific characteristics. Digestion with deoxyribonuclease I (DNase I), S1 nuclease and micrococcal nuclease yield patterns consistent with a triple-helix structure present only in the active state of the promoter. We also demonstrate that the 5'-flanking region of the beta2 gene co-localizes with a CpG island free of methylation in every tissue tested. The results presented here support a role for specific chromatin remodeling events in the regulation of the Na, K-ATPase beta2 gene expression. They also provide the basis for future studies of the transcription factors involved in the regulation of this gene.
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PMID:Chromatin structure analysis of the rat Na, K-ATPase beta2 gene 5'-flanking region. 1194 94

AfsR is a pleiotropic, global regulator that controls the production of actinorhodin, undecylprodigiosin and calcium-dependent antibiotic in Streptomyces coelicolor A3(2). AfsR, with 993 amino acids, is phosphorylated on serine and threonine residues by a protein serine/threonine kinase AfsK and contains an OmpR-like DNA-binding fold at its N-terminal portion and A- and B-type nucleotide-binding motifs in the middle of the protein. The DNA-binding domain, in-dependently of the nucleotide-binding domain, contributed the binding of AfsR to the upstream region of afsS that locates immediately 3' to afsR and encodes a 63-amino-acid protein. No transcription of afsS in the DeltaafsR background and restoration of afsS transcription by afsR on a plasmid in the same genetic background indicated that afsR served as a transcriptional activator for afsS. Interestingly, the AfsR binding site overlapped the promoter of afsS, as determined by DNase I protection assay and high-resolution S1 nuclease mapping. The nucleotide-binding domain contributed distinct ATPase and GTPase activity. The phosphorylation of AfsR by AfsK greatly enhanced the DNA-binding activity and modulated the ATPase activity. The DNA-binding ability of AfsR was independent of the ATPase activity. However, the ATPase activity was essential for transcriptional activation of afsS, probably because the energy available from ATP hydrolysis is required for the isomerization of the closed complex between AfsR and RNA polymerase to a transcriptionally competent open complex. Thus, AfsR turns out to be a unique transcriptional factor, in that it is modular, in which DNA-binding and ATPase activities are physically separable, and the two functions are modulated by phosphorylation on serine and threonine residues.
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PMID:afsS is a target of AfsR, a transcriptional factor with ATPase activity that globally controls secondary metabolism in Streptomyces coelicolor A3(2). 1195 95


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