A DNA Region That Complements on Escherichia coli cysG Mutation In Thiobacillus Ferroocxidans

Tsuyoshi Sugio, Hiroyuki Suzuki, Tsuyoshi Tanaka, Shinji Matsugi, Kouji Tanaka, Tadayoshi Kanao, Tatsuo Tano

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Thiobacillus ferrooxidans AP19-3 has a novel NADH-dependent sulfite reductase in the periplasmic space. The gene responsible for the appearance of NADH-dependent sulfite reductase activity was cloned into a vector plasmid pBR322 to give a 5.7-kb hybrid plasmid, pTHS1, which contains a 1.3-kb DNA fragment of T. ferrooxidans API9-3. When pTHS1 was used to transform sulfite reductase deficient E. coli mutants, strain AT2455 (cysG), JM246 (cysl), and AT2427 (cysI), it complemented only the E. coli cysG mutation. Since cysG codes for S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase, the enzyme involved in siroheme synthesis, the results indicate that the DNA region that codes for S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase is present in a T. ferrooxidans 1.3 kb DNA fragment on pTHS1.

Original languageEnglish
Pages (from-to)728-730
Number of pages3
JournalBioscience, biotechnology, and biochemistry
Volume59
Issue number4
DOIs
Publication statusPublished - Jan 1 1995

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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