| pubmed-article:9335287 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9335287 | lifeskim:mentions | umls-concept:C0995754 | lld:lifeskim |
| pubmed-article:9335287 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:9335287 | lifeskim:mentions | umls-concept:C0002712 | lld:lifeskim |
| pubmed-article:9335287 | lifeskim:mentions | umls-concept:C0008145 | lld:lifeskim |
| pubmed-article:9335287 | lifeskim:mentions | umls-concept:C0017362 | lld:lifeskim |
| pubmed-article:9335287 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:9335287 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:9335287 | pubmed:dateCreated | 1997-11-4 | lld:pubmed |
| pubmed-article:9335287 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9335287 | pubmed:abstractText | A regulatory gene, reg1, was identified in Streptomyces lividans. It encodes a 345-amino-acid protein (Reg1) which contains a helix-turn-helix DNA-binding motif in the N-terminal region. Reg1 exhibits similarity with the LacI/GalR family members over the entire sequence. It displays 95% identity with MalR (the repressor of malE in S. coelicolor), 65% identity with ORF-Sl (a putative regulatory gene of alpha-amylase of S. limosus), and 31% identity with CcpA (the carbon catabolite repressor in Bacillus subtilis). In S. lividans, the chromosomal disruption of reg1 affected the expression of several genes. The production of alpha-amylases of S. lividans and that of the alpha-amylase of S. limosus in S. lividans were enhanced in the reg1 mutant strains and relieved of carbon catabolite repression. As a result, the transcription level of the alpha-amylase of S. limosus was noticeably increased in the reg1 mutant strain. Moreover, the induction of chitinase production in S. lividans was relieved of carbon catabolite repression by glucose in the reg1 mutant strain, while the induction by chitin was lost. Therefore, reg1 can be regarded as a pleiotropic regulatory gene in S. lividans. | lld:pubmed |
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| pubmed-article:9335287 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9335287 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9335287 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9335287 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9335287 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9335287 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9335287 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9335287 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9335287 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:9335287 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:9335287 | pubmed:author | pubmed-author:GuérineauMM | lld:pubmed |
| pubmed-article:9335287 | pubmed:author | pubmed-author:NguyenJJ | lld:pubmed |
| pubmed-article:9335287 | pubmed:author | pubmed-author:FrancouFF | lld:pubmed |
| pubmed-article:9335287 | pubmed:author | pubmed-author:VirolleM JMJ | lld:pubmed |
| pubmed-article:9335287 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9335287 | pubmed:volume | 179 | lld:pubmed |
| pubmed-article:9335287 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9335287 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9335287 | pubmed:pagination | 6383-90 | lld:pubmed |
| pubmed-article:9335287 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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