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J. Biochem, 2003, Vol. 133, No. 1 67-74
© 2003 Japanese Biochemical Society

BIOCHEMISTRY

Characterization of Novel Acetyltransferases Found in Budding and Fission Yeasts That Detoxify a Proline Analogue, Azetidine-2-Carboxylic Acid

Michiyo Nomura, Shigeru Nakamori and Hiroshi Takagi+,

Department of Bioscience, Fukui Prefectural University, 4-1-1 Kenjojima, Matsuoka-cho, Fukui 910-1195

We recently found that budding yeast Saccharomyces cerevisiae {Sigma}1278b, but not genome project strain S288C, has a gene conferring resistance to L-azetidine-2-carboxylic acid (AZC), a toxic four-membered ring analogue of L-proline. Also, the gene, designated as MPR1, encodes a novel acetyltransferase that detoxifies AZC via acetylation. We now report the results of subsequent work. On a homology search with MPR1, we detected a gene in fission yeast Schizosaccharomyces pombe. This gene, designated as ppr1+ (pombe MPR1), is responsible for the AZC-resistance of S. pombe as judged from the results of gene disruption and overexpression experiments. Escherichia coli cells expressing ppr1+, like ones expressing MPR1, were resistant to AZC and produced an AZC acetyltransferase. We further found that the enzymes encoded by MPR1 and ppr1+ were homodimers, and catalyzed the acetylation of AZC but not any other L-proline–related compounds. Ppr1p was more thermostable than Mpr1p, although Ppr1p had a lower optimum temperature than Mpr1p. The higher AZC acetylation activity of Mpr1p, in comparison to that of Ppr1p, was attributed to the larger kcat/Km value for acetyl-CoA of Mpr1p than that of Ppr1p.

+ To whom correspondence should be addressed. Tel: +81-776-61-6000, Fax: +81-776-61-6015, E-mail: hiro{at}fpu.ac.jp


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