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)

The complete nucleotide sequence of the beta-xylosidase gene (xynB) of Bacillus pumilus IPO and its flanking regions was established. A 1617-bp open reading frame for beta-xylosidase, a homodimer enzyme, was observed. The amino acid sequence of the N-terminal region and the molecular mass 62607 Da) of the beta-xylosidase subunit, deduced from the DNA sequence, agreed with the result obtained with the purified enzyme. The Shine-Dalgarno sequence was found 8 bp upstream of the initiation codon, ATG. The xylanase gene (xynA) of the same strain was 4.6 kbp downstream of the 3' end of xynB, and its DNA sequence was reported in our previous paper [Fukusaki, E., Panbangred, W., Shinmyo, A. & Okada, H. (1984) FEBS Lett. 171, 197-201]. The results of the Northern hybridization suggested that the mRNA of xynA and xynB were produced separately. The 5' and 3' ends of the xynA and xynB gene were mapped with nuclease S1. The '-10' regions for promoter sequences of both genes were similar to the consensus sequence for B. subtilis RNA polymerases, the '-35' regions were different from all the known promoters for B. subtilis RNA polymerases.
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PMID:Structure and expression of genes coding for xylan-degrading enzymes of Bacillus pumilus. 244 Jun 80

Protein HU was purified from the cyanobacterium Anabaena 7120. Its complete amino acid sequence was determined by automated Edman degradation of the whole protein and of CNBr and chymotryptic peptides. The active DNA-binding protein is a homodimer of 94-amino acid subunits. Approximately half of the residues are identical to those of the two subunits of HU protein from E. coli. The protein binds to both supercoiled and relaxed double-stranded DNA, cooperatively. The contour lengths of circular DNAs were reduced up to six-fold by HU binding at low ratios of HU to DNA. At higher ratios, highly condensed aggregates were observed. Heterocysts are cells specialized for nitrogen fixation that differentiate at regular intervals along the filaments of Anabaena when they are transferred to a medium lacking combined nitrogen. Protein HU, labeled with 35S in cells growing on ammonia, disappears from developing heterocysts, although it is stably maintained in the intervening strings of vegetative cells. Following establishment of the heterocyst pattern, in which the differentiated cells are spaced about ten cells apart, HU is synthesized in the vegetative cells but not in the heterocysts. Several other vegetative cell DNA-binding proteins are also degraded during the differentiation. The major DNA-binding protein in heterocysts is a new one of subunit molecular mass around 12,000, whose relationship to other DNA-binding proteins is unknown. The gene encoding protein HU was cloned from Anabaena DNA and sequenced. The gene sequence is consistent with the amino acid sequence determined previously. Low stringency hybridization to Anabaena DNA digests suggest that there is a single gene for HU, consistent also with the unique amino acid sequence. S1 nuclease protection experiments suggest that the HU gene promoter differs from those of other Anabaena genes determined to date.
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PMID:Protein HU from the cyanobacterium Anabaena. 774 31