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Journal of Bacteriology, May 2005, p. 2957-2966, Vol. 187, No. 9
0021-9193/05/$08.00+0     doi:10.1128/JB.187.9.2957-2966.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Changes in the Extracellular Proteome Caused by the Absence of the bldA Gene Product, a Developmentally Significant tRNA, Reveal a New Target for the Pleiotropic Regulator AdpA in Streptomyces coelicolor

Dae-Wi Kim,1,2 Keith Chater,1 Kye-Joon Lee,2 and Andy Hesketh1*

Department of Molecular Microbiology, John Innes Centre, Norwich Research Park, Colney, Norwich, United Kingdom,1 School of Biological Sciences, Seoul National University, Seoul, Republic of South Korea2

Received 20 December 2004/ Accepted 25 January 2005

The extracellular proteome of Streptomyces coelicolor grown in a liquid medium was analyzed by using two-dimensional gel electrophoresis and matrix-assisted laser desorption ionization-time of flight peptide mass fingerprint analysis. Culture supernatants became protein rich only after rapid growth had been completed, supporting the idea that protein secretion is largely a stationary phase phenomenon. Out of about 600 protein spots observed, 72 were characterized. The products of 47 genes were identified, with only 11 examples predicted to be secreted proteins. Mutation in bldA, previously known to impair the stationary phase processes of antibiotic production and morphological differentiation, also induced changes in the extracellular proteome, revealing even greater pleiotropy in the bldA phenotype than previously known. Four proteins increased in abundance in the bldA mutant, while the products of 11 genes, including four secreted proteins, were severely down-regulated. Although bldA encodes the only tRNA capable of efficiently translating the rare UUA (leucine) codon, none of the latter group of genes contains an in-frame TTA. SCO0762, a serine-protease inhibitor belonging to the Streptomyces subtilisin inhibitor family implicated in differentiation in other streptomycetes, was completely absent from the bldA mutant. This dependence was shown to be mediated via the TTA-containing regulatory gene adpA, also known as bldH, a developmental gene that is responsible for the effects of bldA on differentiation. Mutation of the SCO0762 gene abolished detectable trypsin-protease inhibitory activity but did not result in any obvious morphological defects.

* Corresponding author. Mailing address: Department of Molecular Microbiology, John Innes Centre, Colney Lane, Norwich NR4 7UH, United Kingdom. Phone: (44) 1603 450757. Fax: (44) 1603 450778. E-mail: andrew.hesketh{at}bbsrc.ac.uk.

Journal of Bacteriology, May 2005, p. 2957-2966, Vol. 187, No. 9
0021-9193/05/$08.00+0     doi:10.1128/JB.187.9.2957-2966.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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