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   <subfield code="a">Individual Expression of Candida tropicalis Peroxisomal and Mitochondrial Carnitine Acetyltransferase-Encoding Genes and Subcellular Localization of the Products in Saccharomyces cerevisiae</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Hiroyuki Kawachi, Haruyuki Atomi, Mitsuyoshi Ueda, Noriko Hashimoto, Keiko Kobayashi, Tomoko Yoshida, Naomi Kamasawa, Masako Osumi, Atsuo Tanaka]</subfield>
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   <subfield code="a">In an n-alkane-assimilating yeast, Candida tropicalis, carnitine acetyltransferase (CAT; EC 2.3.1.7) was localized in both peroxisomes and mitochondria. Both CATs were encoded by one gene, CT-CAT, although the initiation sites of translation were suggested to be different. In the present study, the genes corresponding to the supposed C. tropicalis peroxisomal and mitochondrial CATs, which were truncated from the CT-CAT gene, were individually expressed in Saccharomyces cerevisiae, using the C. tropicalis isocitrate lyase promoter (UPR-ICL), which is inducible by oleic acid in concert with proliferation of peroxisomes in S. cerevisiae [Umemura, K., Atomi, H., Kanai, T., Teranishi, Y., Ueda, M., and Tanaka, A. (1995) Appl. Microbiol. Biotechnol. 43, 489-492]. The 71 kDa precursor of mitochondrial CAT, initiating at the first Met, was found to be processed to the mature size (66 kDa) in S. cerevisiae and immunoelectronmicroscopical observation revealed that this enzyme was localized in mitochondria. On the other hand, 68 kDa CAT, initiating at the second Met (residue No. 19), had no cleavable signal and was translocated into peroxisomes and cytosol, but not into mitochondria. The aniino-terniinal amino acid sequences of individually expressed CATs were identical to those of CATs isolated from alkane-grown C. tropicalls cells, respectively. These results demonstrated that only the 71 kDa protein yielded the 66 kDa protein and that peroxisomal and mitochondrial CATs arose from the difference in the initiation sites of translation.</subfield>
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   <subfield code="a">© 1996 BY THE JOURNAL OF BIOCHEMISTRY</subfield>
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   <subfield code="a">Regular Papers</subfield>
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   <subfield code="a">Candida tropicalis</subfield>
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   <subfield code="a">initiation of traslation</subfield>
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   <subfield code="a">Kawachi</subfield>
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   <subfield code="u">Laboratory of Applied Biological Chemistry, Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University Yoshida, Sakyo-ku, Kyoto 606-01</subfield>
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   <subfield code="a">Atomi</subfield>
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   <subfield code="u">Laboratory of Applied Biological Chemistry, Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University Yoshida, Sakyo-ku, Kyoto 606-01</subfield>
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   <subfield code="a">Ueda</subfield>
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   <subfield code="u">Laboratory of Applied Biological Chemistry, Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University Yoshida, Sakyo-ku, Kyoto 606-01</subfield>
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   <subfield code="a">Hashimoto</subfield>
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   <subfield code="u">Department of Chemical and Biological Sciences, Faculty of Science, Japan Women's University Mejiro-dai, Bunkyo-ku, Tokyo 112</subfield>
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   <subfield code="a">Kobayashi</subfield>
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   <subfield code="a">Yoshida</subfield>
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   <subfield code="t">The Journal of Biochemistry</subfield>
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   <subfield code="g">120/4(1996-10), 731-735</subfield>
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