Open AccessBinding study of AfsK, a Ser/Thr kinase from Streptomyces coelicolor A3(2) and S ‐adenosyl‐ l ‐methionine
Author(s) -
Lee Yukyung,
Kim Kwangsoo,
Suh JooWon,
Rhee Sangkee,
Lim Yoongho
Publication year - 2007
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2006.00531.x
Subject(s) - streptomyces coelicolor , actinorhodin , biochemistry , streptomyces , stereochemistry , biology , streptomycetaceae , actinomycetales , chemistry , bacteria , genetics
Streptomyces coelicolor A3(2) produces an antibiotic, actinorhodin, which belongs to the aromatic polyketides and which can function as an acid/base indicator. Its production results in the death of microorganisms in the vicinity of S. coelicolor A3(2), and this phenomenon can be used in concert with biopesticides. The exogenous addition of S ‐adenosyl‐ l ‐methionine (SAM) to S. coelicolor A3(2) enhances its actinorhodin production and may initiate actinorhodin biosynthesis, with at least four genes being involved. Of these (because afsK initiates the others), AfsK, the protein expressed from afsK , may be interacting with SAM. Although the three‐dimensional structure of AfsK has not been determined, the differences between nuclear magnetic resonance (NMR) signals obtained from the free form of SAM and those from a SAM–protein complex can help us to determine whether SAM binds to the C‐terminal of AfsK or not. In the present study, NMR data analysis strongly supported the idea that SAM binds to AfsK.