Self-activation of serine/threonine kinase AfsK on autophosphorylation at threonine-168

The Journal of Antibiotics
Ayami TomonoS Horinouchi

Abstract

A Hanks-type protein kinase AfsK autophosphorylates on threonine residue(s) and phosphorylates AfsR, a global regulator for secondary metabolism in Streptomyces coelicolor A3(2). Mass spectrometry of a tryptic digest of the autophosphorylated form of AfsK deltaC corresponding to the kinase catalytic domain (Met-1 to Arg-311) of AfsK, together with subsequent site-directed mutagenesis of the candidate amino acids, identified threonine-168 as a single autophosphorylation site. Threonine-168 is located in the activation loop that is known for some Ser/Thr kinases to modulate kinase activity on phosphorylation of one or more threonine residues within the loop. Consistent with this, mutant T168D, in which Thr-168 was replaced by Asp, became a constitutively active kinase; it phosphorylated AfsR to the same extent as AfsK deltaC produced in and purified from Escherichia coli cells during which a considerable population of it had been already phosphorylated intermolecularly. All these findings show that autophosphorylation or intermolecular phosphorylation of threonine-168 in AfsK accounts for the self-activation of its kinase activity.

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Citations

Aug 8, 2012·Proceedings of the National Academy of Sciences of the United States of America·Antje M HempelKlas Flärdh
Feb 8, 2007·Bioscience, Biotechnology, and Biochemistry·Sueharu Horinouchi
Mar 8, 2008·Bioscience, Biotechnology, and Biochemistry·Hiroaki UrabeKiyoto Motojima
May 26, 2011·Natural Product Reports·Gilles P van Wezel, Kenneth J McDowall
Dec 20, 2019·Applied Microbiology and Biotechnology·Qin LiuJing He
May 5, 2021·Microbiology·Vanessa Yoon CalveloJustin Rea Nodwell

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