The α-Aminoadipate Pathway for Lysine Biosynthesis Is Widely Distributed among Thermus Strains

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概要

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• We previously reported that lysine is synthesized through the α-aminoadipate pathway in Thermus thermophilus HB27 (T.Kosuge and T.Hoshino, FEMS Microbiol.Lett., 169, 361-367, 1998), which was the first report demonstrating the synthesis of lysine through the α-aminoadipate pathway in Bacteria. LYS20 and LYS4, which respectively encode homocitrate synthase and homoaconitate hydratase have already been identified as the lysine biosynthetic genes in T.thermophilus HB27. In the present work, we examined eight other Thermus strains for the existence of genes belonging to the α-aminoadipate pathway. BamHI- or BglII-digested total DNAs from the eight strains were analyzed by Southern hybridization using LYS20 or LYS4 as a DNA probe. DNA fragments that hybridized with one or both of the genes were detected in seven of the Thermus strains but not in T.ruber. The sizes of the fragments that hybridized with the LYS20 and LYS4 probes were the same among T.thermophilus HB27, T.thermophilus HB8, "T.caldophilus" GK24, and four "T.flavus" strains. For example, a similar 4.3-kb fragment was detected in each of the above seven strains. In this fragment, four open reading frames were found downstream of the LYS4 gene in T.thermophilus HB27. Gene disruption experiments revealed that three open reading frames are involved in lysine biosynthesis in T.thermophilus HB27. These results strongly suggest that the lysine biosynthetic gene cluster for the α-aminoadipate pathway is widely distributed in the genus Thermus.

• 社団法人日本生物工学会の論文
• 1999-12-25

著者

• Hoshino Takayuki

  Institute Of Applied Biochemistry University Of Tsukuba

• KOSUGE TAKEHIDE

  Institute of Applied Biochemistry, University of Tsukuba

• Kosuge Takehide

  Institute Of Applied Biochemistry University Of Tsukuba

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• Overproduction of Carotenoids in Thermus thermophilus
• Isolation and Partial Characterization of Carotenoid Underproducing and Overproducing Mutants from an Extremetly Thermophilic Thermus thermophilus HB27
• Fusion with Ribosomal Protein L32 Increased the in vivo Thermostability of Kanamycin Nucleotidyltransferase in Thermus thermophilus
• The α-Aminoadipate Pathway for Lysine Biosynthesis Is Widely Distributed among Thermus Strains
• Cloning and Sequence Analysis of Fumarase and Superoxide Dismutase Genes from an Extreme Thermophile Thermus thermophilus HB27
• Efficient Selection for Thermostable Protease in Themus thermophilus
• Plasmid Marker Rescue Transformation in Thermus thermophilus
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