Molecular and functional analysis of the ribosomal L11 and S12 protein genes ( rplK and rpsL ) of Streptomyces coelicolor A3(2) |
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Authors: | K Ochi D Zhang S Kawamoto and A Hesketh |
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Institution: | (1) National Food Research Institute, 2-1-2 Kannondai, Tsukuba, Ibaraki 305, Japan Fax: +81-298-38-7996; e-mail: kochi@ss.nfri.affrc.go.jp, JP |
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Abstract: | A RelC deletion mutant, KO-100, of Streptomyces coelicolor A3(2) has been isolated from a collection of spontaneous thiostrepton-resistant mutants. KO-100 grows as vigorously as the
parent strain and possesses a 6-bp deletion within the rplK, previously termed relC. When the wild-type rplK gene was propagated on a low-copy-number vector in mutant KO-100, the ability to produce ppGpp, actinorhodin and undecylprodigiosin,
which had been lost in the RelC mutant, was completely restored. Allele replacement by gene homogenotization demonstrated
that the RelC mutation is responsible for the resistance to thiostrepton and the inactivation of ppGpp, actinorhodin and undecylprodigiosin
production. Western blotting showed that ribosomes from the RelC mutant KO-100 contain only one-eighth the amount of L11 protein
found in ribosomes of the parent strain. The impairment of antibiotic production in KO-100 could be rescued by the introduction
of mutations that confer resistance to streptomycin (str), which result in alteration of Lys-88 in ribosomal protein S12 to Glu or Arg. No accompanying restoration of ppGpp synthesis
was detected in these RelC str double mutants.
Received: 12 May 1997 / Accepted: 22 July 1997 |
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Keywords: | Stringent response Ribosomal proteins rplK rpsL Streptomyces coelicolor |
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