Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
2002-10-10
pubmed:abstractText
In Streptomyces griseus, A-factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone) switches on aerial mycelium formation and secondary metabolite biosynthesis. An A-factor-dependent transcriptional activator, AdpA, activates multiple genes required for morphological development and secondary metabolism in a programmed manner. A region upstream of a zinc-containing metalloendopeptidase gene (sgmA) was found among the DNA fragments that had been isolated as AdpA-binding sites. The primary product of sgmA consisted of N-terminal pre, N-terminal pro, mature, and C-terminal pro regions. sgmA was transcribed in an AdpA-dependent manner, and its transcription was markedly enhanced at the timing of aerial mycelium formation. AdpA bound two sites in the region upstream of the sgmA promoter; one was at about nucleotide position -60 (A site) with respect to the transcriptional start point of sgmA, and the other was at about position -260 (B site), as determined by DNase I footprinting. Transcriptional analysis with mutated promoters showed that the A site was essential for the switching on of sgmA transcription and that the B site was necessary for the marked enhancement of transcription at the timing of aerial mycelium formation. Disruption of the chromosomal sgmA gene resulted in a delay in aerial hypha formation by half a day. SgmA is therefore suggested to be associated with the programmed morphological development of Streptomyces, in which this peptidase, perhaps together with other hydrolytic enzymes, plays a role in the degradation of proteins in substrate hyphae for reuse in aerial hypha formation.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-10225953, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-10339816, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-10400660, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-10540289, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-10913094, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-11832504, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-1444261, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-1549509, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-1769959, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-1938623, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-3096818, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-3410319, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-3891055, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-5488465, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-6246368, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-6295884, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-6313861, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-6415235, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-6429133, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-7504906, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-7934895, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-821930, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-8690707, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-8981988, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-9573206, http://linkedlifedata.com/resource/pubmed/commentcorrection/12374836-9720222
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9193
pubmed:author
pubmed:issnType
Print
pubmed:volume
184
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6016-25
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:12374836-4-Butyrolactone, pubmed-meshheading:12374836-Amino Acid Sequence, pubmed-meshheading:12374836-Bacterial Proteins, pubmed-meshheading:12374836-Base Sequence, pubmed-meshheading:12374836-Binding Sites, pubmed-meshheading:12374836-Cloning, Molecular, pubmed-meshheading:12374836-DNA, Bacterial, pubmed-meshheading:12374836-DNA Footprinting, pubmed-meshheading:12374836-DNA-Binding Proteins, pubmed-meshheading:12374836-Deoxyribonuclease I, pubmed-meshheading:12374836-Genes, Bacterial, pubmed-meshheading:12374836-Metalloendopeptidases, pubmed-meshheading:12374836-Molecular Sequence Data, pubmed-meshheading:12374836-Nucleotides, pubmed-meshheading:12374836-Phenotype, pubmed-meshheading:12374836-Sequence Analysis, DNA, pubmed-meshheading:12374836-Streptomyces griseus, pubmed-meshheading:12374836-Trans-Activators, pubmed-meshheading:12374836-Transcription, Genetic, pubmed-meshheading:12374836-Transcriptional Activation, pubmed-meshheading:12374836-Zinc Fingers
pubmed:year
2002
pubmed:articleTitle
Control by A-factor of a metalloendopeptidase gene involved in aerial mycelium formation in Streptomyces griseus.
pubmed:affiliation
Department of Biotechnology, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't