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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2000-12-29
pubmed:abstractText
WD-repeat proteins are found in all eukaryotes and are implicated in a variety of regulatory functions as a result of protein-protein interactions. PkwA from Thermomonospora curvata CCM3352 is a first potential example of a WD-repeat protein in a prokaryotic actinomycete. A mAb (3G2) was generated against the carboxy terminus of PkwA and was used to analyse the expression of PkwA in T. curvata. PkwA was detected in exponential growth phase following inoculation with spores, but could not be found at any stage of growth following inoculation with vegetative mycelium. PkwA and its WD domain were expressed in Escherichia coli as His-tag derivatives and purified on a Talon metal affinity matrix. The WD domain was phosphorylated by Pkg2, a membrane-spanning protein Ser/Thr kinase from 'Streptomyces granaticolor'. A membrane fraction from an exponential, spore-derived culture of T. curvata was found to phosphorylate the WD domain specifically in the presence of Mn(2+). These data confirm that PkwA is expressed in spore-derived exponential growth phase of T. curvata and could play a role as a molecular switch in a signalling pathway.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1350-0872
pubmed:author
pubmed:issnType
Print
pubmed:volume
146 Pt 12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3259-67
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
PkwA, a WD-repeat protein, is expressed in spore-derived mycelium of Thermomonospora curvata and phosphorylation of its WD domain could act as a molecular switch.
pubmed:affiliation
Laboratory of Physiology and Genetics of Actinomycetes, Institute of Microbiology, AS CR, Videnska 1083, 142 20, Prague-4, Czech Republic.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't