Cloning of the gene encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase from terpenoid antibiotic-producing Streptomyces strains |
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Authors: | Dairi T Motohira Y Kuzuyama T Takahashi S Itoh N Seto H |
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Institution: | (1) Biotechnology Research Center, Toyama Prefectural University, Toyama 939-0398, Japan, JP;(2) Institute of Molecular and Cellular Biosciences, University of Tokyo, Bunkyo-ku, 113-0032, Japan E-mail: haseto@imcbns.iam.u-tokyo.ac.jp Tel.: +81-3-58417839; Fax: +81-3-58418485, JP |
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Abstract: | We have isolated a mutant lacking 3-hydroxy-3-methylglutaryl CoA (HMG-CoA) reductase activity from a terpenoid antibiotic
(terpentecin) producer, Streptomyces griseolosporeus MF730-N6, which uses both the mevalonate and nonmevalonate pathways for the formation of isopentenyl diphosphate, by screening
terpentecin non-producing mutants. Terpentecin is known to be synthesized via the mevalonate pathway. The gene encoding HMG-CoA
reductase (hmgg) was cloned and identified by complementation of the mutant, using a self-cloning system developed in this study for strain
MF730-N6. The corresponding hmgs gene for HMG-CoA reductase was also cloned from Streptomyces sp. KO-3988, which produces the terpenoid antibiotic furaquinocin. Sequence analysis of hmgg and hmgs showed that both genes encode polypeptides of 353 amino acids which are 84% identical to each other. A search of protein
sequence databases revealed that both gene products were also similar to HMG-CoA reductases from a variety of other organisms,
including Streptomyces sp. CL190 (hmgg is 89% and hmgs 85% identical to its CL190 homolog), sea urchin (40.3 and 40.5%), German cockroach (37.6 and 38.4%), and Camptotheca acuminata (39.7 and 40.8%).
Received: 17 May 1999 / Accepted: 10 September 1999 |
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Keywords: | Mevalonate pathway HMG-CoA reductase Prokaryote Streptomyces Terpentecin |
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