Linked Life Data

18266739

Source:http://linkedlifedata.com/resource/pubmed/id/18266739

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2008-2-26
pubmed:abstractText
Homogentisate 1,2-dioxygenase (HmgA) converts homogentisate to maleylacetoacetate in the pathway of tyrosine catabolism in living organisms. Studies published to date have not elucidated the transcriptional regulation of hmgA and its biological function in Streptomyces spp. Here it is shown that the transcription of hmgA in Streptomyces coelicolor was activated by HpdA, an AsnC-type activator, in the presence of tyrosine. Disruption of hmgA led to enhanced production of diffusible brown pigment, suggesting that hmgA is required for tyrosine catabolism in Streptomyces coelicolor. The production of actinorhodin in the hmgA disruption mutant was several fold higher than that in the wild-type strain (M145), indicating that hmgA of tyrosine catabolism correlates with actinorhodin biosynthesis. Furthermore, S1 mapping showed that the transcription of actII-ORF4, a pathway-specific activator gene of actinorhodin biosynthesis, was increased in the hmgA disruption mutant. These results reveal the transcriptional regulation of hmgA and the positive contribution of hmgA disruption to the actinorhodin biosynthesis in Streptomyces coelicolor.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0378-1097
pubmed:author
pubmed:issnType
Print
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
219-25
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
hmgA, transcriptionally activated by HpdA, influences the biosynthesis of actinorhodin in Streptomyces coelicolor.
pubmed:affiliation
State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't