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

Changes in calcium levels control the differentiation of skin epithelial cells and thus may also affect the epithelial cells of the hair follicle. We have isolated a murine cDNA clone, pCAL-F559, for the calcium-binding protein calcyclin by differential screening of a cDNA library made from RNA isolated from hair follicles of 6-d-old mice. The identity of our cDNA clone was established by comparing the DNA sequence with the sequence of the human calcyclin gene. That the authentic calcyclin mRNA encoded by pCAL-559 is present in skin of 3-d-old mice was confirmed by S1 nuclease protection assays. As measured by RNA dot blots, calcyclin mRNA levels in the skin change in accordance with the hair cycle and reaches a peak a few days prior to the mRNA for structural hair proteins. Although we can demonstrate by in situ hybridization that mRNA for calcyclin is localized in the post-mitotic keratogenous region of the hair follicle we can only assume that this calcium binding protein is involved in the control of differentiation of these cells by regulating their Ca++ levels.
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PMID:Expression of calcyclin, a calcium-binding protein, in the keratogenous region of growing hair follicles. 200 57

The structural organization of the entire rat vitamin-D-dependent calcium-binding protein (9-kDa CaBP) gene was determined by analysis of overlapping genomic clones isolated from a rat genomic library using the rat 9-kDa CaBP cDNA [Desplan C., Heidmann O., Lillie J., Auffray C. and Thomasset M. (1983) J. Biol. Chem. 258, 13502-13505]. These clones together span 30 kbp of rat genomic DNA, with the rat 9-kDa CaBP gene lying in the middle. The 9-kDa CaBP gene is 2.5 kbp long and contains three exons interrupted by two introns. The first exon contains almost the entire 5' untranslated region. The second exon codes for the calcium-binding site I, the third exon codes for site II and the 3' untranslated region. Therefore each of the calcium-binding domains is encoded by single, separate exons. The transcription initiation site was identified by S1 nuclease mapping and primer extension. A consensus sequence TATAAA is localized 31 bp upstream from the cap site and the 'CCAAT-box' lies upstream from the transcription start. Single (AC)25 and (AG)23 repeats are present in the second intron together with an Alu-like sequence. Repetitive elements are present 5 kbp upstream from the cap site and in the 3' flanking region. Comparison of the known rat CaBP sequences (9-kDa CaBP, 28-kDa CaBP, S100 protein) shows that the 9-kDa CaBP is more closely related to the S100 protein than to the 28-kDa CaBP. There is no evidence to indicate that 9-kDa CaBP has arisen from the 28-kDa CaBP.
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PMID:The rat vitamin-D-dependent calcium-binding protein (9-kDa CaBP) gene. Complete nucleotide sequence and structural organization. 334 61

Vitamin D-dependent 28-kDa calcium-binding protein (CaBP28) cDNA clones were isolated from a chicken intestinal library. The nucleotide sequence analysis of the CaBP28 cDNA shows an open reading frame of 786 nucleotides, coding for a 262-amino acid 30.167-kDa protein. Interestingly, the protein contains six repeats of a domain with the feature of a calcium-binding site. In two of the six domains, oxygen-containing amino acids important for the positioning of calcium are absent, suggesting that these two sites have lost their calcium-binding capability and might have adopted a new function in evolution. In the chicken intestine, three different sized species of CaBP28 mRNA (2.0, 2.8, and 3.1 kilobases) are detected. Primer extension and S1 nuclease mapping show that the three CaBP28 mRNA species share a common 5' end but differ in the length of their 3' noncoding sequence. A similar triplet of CaBP28 mRNAs is identified in the rat kidney by the chicken probe, showing an interspecies conservation of the CaBP28. In the rat intestine, however, no CaBP28 mRNA could be detected. Instead, a vitamin D-dependent 9-kDa CaBP (CaBP9) is expressed, with an mRNA size of approximately equal to 0.7 kilobase that does not cross-hybridize with the CaBP28 probe. This indicates that the CaBP28 and CaBP9 are the product of two independent genes.
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PMID:The 28-kDa vitamin D-dependent calcium-binding protein has a six-domain structure. 346 88

A gene (cabA) encoding a calcium-binding protein was cloned from Streptomyces ambofaciens. CabA was 180 amino acid residues long and contained four typical EF-hand motifs bearing high sequence similarity to the calcium-binding sites in calmodulin. Consistent with this, CabA showed distinct calcium-binding activity, comparable to bovine brain calmodulin. cabA was transcribed throughout growth, as found by S1 nuclease mapping. Southern hybridization experiments showed that a single copy of cabA was present in various Streptomyces species. A hypothetical relationship between CabA and aerial mycelium formation in this strain was examined, since S. ambofaciens showed calcium-dependent aerial mycelium formation. However, disruption of cabA or overexpression of cabA in S. ambofaciens caused no detectable phenotypic changes.
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PMID:A calcium-binding protein with four EF-hand motifs in Streptomyces ambofaciens. 1127 20