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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1992-2-18
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S55527,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S55528,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S55529,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S55530,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S55531,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S55532,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S63909,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S69885,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S75682,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X58833
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
|
pubmed:issn |
0026-8925
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
230
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pubmed:geneSymbol |
act
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
401-12
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1766437-Amino Acid Sequence,
pubmed-meshheading:1766437-Anthraquinones,
pubmed-meshheading:1766437-Anti-Bacterial Agents,
pubmed-meshheading:1766437-Base Sequence,
pubmed-meshheading:1766437-Cloning, Molecular,
pubmed-meshheading:1766437-Genes, Bacterial,
pubmed-meshheading:1766437-Genetic Complementation Test,
pubmed-meshheading:1766437-Molecular Sequence Data,
pubmed-meshheading:1766437-Multigene Family,
pubmed-meshheading:1766437-Mutation,
pubmed-meshheading:1766437-Open Reading Frames,
pubmed-meshheading:1766437-Plasmids,
pubmed-meshheading:1766437-Restriction Mapping,
pubmed-meshheading:1766437-Streptomyces
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pubmed:year |
1991
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pubmed:articleTitle |
Organisation and functions of the actVA region of the actinorhodin biosynthetic gene cluster of Streptomyces coelicolor.
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pubmed:affiliation |
John Innes Institute, John Innes Centre, Norwich, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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