Phosphorylation of AfsR by multiple serine/threonine kinases in Streptomyces coelicolor A3(2)

Reiko, Sawai and Ayano, Suzuki and Yuji, Takano and Lee, Ping Chin and Sueharu, Horinouchi (2004) Phosphorylation of AfsR by multiple serine/threonine kinases in Streptomyces coelicolor A3(2). Gene, 334 (1-2). pp. 53-61. ISSN 0378-1119

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Abstract

AfsK, a protein serine/threonine kinase, autophosphorylates on serine and threonine residues and phosphorylates serine and threonine residues of AfsR, a transcriptional activator for afsS involved in secondary metabolism in Streptomyces coelicolor A3(2). pkaG encoding a 592-amino-acid protein and SCD10.09 (named afsL) encoding a 580-amino-acid protein, both of which encode an AfsK-like protein, were transcribed throughout growth. PkaG with a histidine-tag and the kinase catalytic domain of PkaG, produced in Escherichia coli, autophosphorylated dominantly on threonine and slightly on serine residues. In addition, these proteins phosphorylated AfsR on threonine and serine residues. The catalytic domain of AfsL also autophosphorylated and phosphorylated AfsR, on threonine and serine residues in both cases. AfsR was thus found to be phosphorylated by multiple kinases. Disruption of the chromosomal pkaG gene resulted in slightly reduced production of the pigmented antibiotic actinorhodin. These findings, together with the presence of about 40 AfsK homologues and at least five AfsR homologues in S. coelicolor A3(2), suggest that the regulatory networks via eukaryotic-type protein phosphorylation are more diverse and versatile than we have expected.

Item Type: Article
Uncontrolled Keywords: Actinorhodin, Amino acid(s), Antibiotic production, Base pair(s), PCR, polymerase chain reaction, Signal transduction, Transcriptional factor
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: SCHOOL > School of Science and Technology
Depositing User: Unnamed user with email storage.bpmlib@ums.edu.my
Date Deposited: 22 Feb 2012 08:52
Last Modified: 16 Oct 2017 07:26
URI: http://eprints.ums.edu.my/id/eprint/3576

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