pubmed-article:1766437 | rdf:type | pubmed:Citation | lld:pubmed |
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pubmed-article:1766437 | lifeskim:mentions | umls-concept:C0050663 | lld:lifeskim |
pubmed-article:1766437 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:1766437 | pubmed:dateCreated | 1992-2-18 | lld:pubmed |
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pubmed-article:1766437 | pubmed:abstractText | Sequence analysis of the actVA region of the actinorhodin biosynthetic gene cluster of Streptomyces coelicolor revealed a succession of six open reading frames (ORFs), all running in the same direction and extending over 5.32 kb. The protein product of actVA-ORF1 strongly resembles that of another gene, elsewhere in the act cluster (actII-ORF2), which codes for a trans-membrane protein previously implicated in actinorhodin export from the mycelium. This suggests that the two gene products may co-operate in actinorhodin export, perhaps being sufficient for self-protection of the organism against suicide. At least four of the other five ORFs are implicated in the control of the C-6 and C-8 ring-hydroxylation reactions, lacking in actVA mutants, that occur at middle to late stages in the actinorhodin biosynthetic pathway. This conclusion was reached by genetic mapping of actVA mutants to actVA-ORF3 and -ORF5 (and perhaps -ORF4), and by the finding of strong resemblances between the protein products of actVA-ORF2 and -ORF6 and the products of genes of the oxytetracycline or tetracenomycin gene clusters that have been implicated in ring-hydroxylation reactions in the biosynthesis of these other aromatic polyketide antibiotics. | lld:pubmed |
pubmed-article:1766437 | pubmed:language | eng | lld:pubmed |
pubmed-article:1766437 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1766437 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1766437 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1766437 | pubmed:month | Dec | lld:pubmed |
pubmed-article:1766437 | pubmed:issn | 0026-8925 | lld:pubmed |
pubmed-article:1766437 | pubmed:author | pubmed-author:HopwoodD ADA | lld:pubmed |
pubmed-article:1766437 | pubmed:author | pubmed-author:MartinezEE | lld:pubmed |
pubmed-article:1766437 | pubmed:author | pubmed-author:MalpartidaFF | lld:pubmed |
pubmed-article:1766437 | pubmed:author | pubmed-author:CaballeroJ... | lld:pubmed |
pubmed-article:1766437 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1766437 | pubmed:volume | 230 | lld:pubmed |
pubmed-article:1766437 | pubmed:geneSymbol | act | lld:pubmed |
pubmed-article:1766437 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1766437 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1766437 | pubmed:pagination | 401-12 | lld:pubmed |
pubmed-article:1766437 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:1766437 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:1766437 | pubmed:articleTitle | Organisation and functions of the actVA region of the actinorhodin biosynthetic gene cluster of Streptomyces coelicolor. | lld:pubmed |
pubmed-article:1766437 | pubmed:affiliation | John Innes Institute, John Innes Centre, Norwich, UK. | lld:pubmed |
pubmed-article:1766437 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1766437 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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