Comparison of molecular structures and regulation of biosynthesis of unique thiolase isozymes localized only in peroxisomes of n-alkane-utilizable yeast, Candida tropicalis

Naoki Kanayama, Mitsuyoshi Ueda, Haruyuki Atom, Tatsuo Kurihara, Jun Kondo, Yutaka Teranishi, Atsuo Tanaka

Research output: Contribution to journalArticle

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Abstract

Two transcribed genes encoding 3-ketoacyl-CoA thiolase [(EC 2.3.1.16) Thiolase III], one of the peroxisomal thiolase isozymes, of n-alkane-utilizable yeast, Candida tropicalis, were isolated. Restriction maps of these two genes were very similar. Each of the genes had only one open reading frame consisting of 1224 bp corresponding to 408 amino acid residues. The nucleotide sequences of another thiolase isozyme in peroxisomes of C. tropicalis, acetoacetyl-CoA thiolase (Thiolase IA and IB), have been already determined (Kurihara et al., Eur. J. Biochem., 210, 999-1005, 1992). The amino acid sequences of these peroxisomal thiolase isozymes (Thiolases I and III) showed 35% homology. The regulation of biosynthesis of these thiolases in C. tropicalis was compared by RNA and Western blotting analyses. The results revealed that the biosynthesis of Thiolase III in C. tropicalis was strongly induced in a medium containing butyrate or alkanes as a carbon source and a peroxisome proliferator, while Thiolase I was constitutively expressed even in a medium with glucose or acetate, although a slight induction was observed at the levels of transcription and translation in the medium containing butyrate or alkanes. Thus, the regulations of biosyntheses of Thiolases I and III were found to be quite different, in spite of the enzymes in the final step of the peroxisomal fatty acid β-oxidation system.

Original languageEnglish
Pages (from-to)273-278
Number of pages6
JournalJournal of Fermentation and Bioengineering
Volume78
Issue number4
DOIs
Publication statusPublished - 1994
Externally publishedYes

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Candida tropicalis
Alkanes
Peroxisomes
Candida
Biosynthesis
Molecular Structure
Yeast
Paraffins
Molecular structure
Isoenzymes
Butyrates
Yeasts
Amino acids
Acetyl-CoA C-Acetyltransferase
Acetyl-CoA C-Acyltransferase
Genes
Peroxisome Proliferators
Amino Acids
Gene encoding
Transcription

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • Bioengineering

Cite this

Comparison of molecular structures and regulation of biosynthesis of unique thiolase isozymes localized only in peroxisomes of n-alkane-utilizable yeast, Candida tropicalis. / Kanayama, Naoki; Ueda, Mitsuyoshi; Atom, Haruyuki; Kurihara, Tatsuo; Kondo, Jun; Teranishi, Yutaka; Tanaka, Atsuo.

In: Journal of Fermentation and Bioengineering, Vol. 78, No. 4, 1994, p. 273-278.

Research output: Contribution to journalArticle

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abstract = "Two transcribed genes encoding 3-ketoacyl-CoA thiolase [(EC 2.3.1.16) Thiolase III], one of the peroxisomal thiolase isozymes, of n-alkane-utilizable yeast, Candida tropicalis, were isolated. Restriction maps of these two genes were very similar. Each of the genes had only one open reading frame consisting of 1224 bp corresponding to 408 amino acid residues. The nucleotide sequences of another thiolase isozyme in peroxisomes of C. tropicalis, acetoacetyl-CoA thiolase (Thiolase IA and IB), have been already determined (Kurihara et al., Eur. J. Biochem., 210, 999-1005, 1992). The amino acid sequences of these peroxisomal thiolase isozymes (Thiolases I and III) showed 35{\%} homology. The regulation of biosynthesis of these thiolases in C. tropicalis was compared by RNA and Western blotting analyses. The results revealed that the biosynthesis of Thiolase III in C. tropicalis was strongly induced in a medium containing butyrate or alkanes as a carbon source and a peroxisome proliferator, while Thiolase I was constitutively expressed even in a medium with glucose or acetate, although a slight induction was observed at the levels of transcription and translation in the medium containing butyrate or alkanes. Thus, the regulations of biosyntheses of Thiolases I and III were found to be quite different, in spite of the enzymes in the final step of the peroxisomal fatty acid β-oxidation system.",
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AB - Two transcribed genes encoding 3-ketoacyl-CoA thiolase [(EC 2.3.1.16) Thiolase III], one of the peroxisomal thiolase isozymes, of n-alkane-utilizable yeast, Candida tropicalis, were isolated. Restriction maps of these two genes were very similar. Each of the genes had only one open reading frame consisting of 1224 bp corresponding to 408 amino acid residues. The nucleotide sequences of another thiolase isozyme in peroxisomes of C. tropicalis, acetoacetyl-CoA thiolase (Thiolase IA and IB), have been already determined (Kurihara et al., Eur. J. Biochem., 210, 999-1005, 1992). The amino acid sequences of these peroxisomal thiolase isozymes (Thiolases I and III) showed 35% homology. The regulation of biosynthesis of these thiolases in C. tropicalis was compared by RNA and Western blotting analyses. The results revealed that the biosynthesis of Thiolase III in C. tropicalis was strongly induced in a medium containing butyrate or alkanes as a carbon source and a peroxisome proliferator, while Thiolase I was constitutively expressed even in a medium with glucose or acetate, although a slight induction was observed at the levels of transcription and translation in the medium containing butyrate or alkanes. Thus, the regulations of biosyntheses of Thiolases I and III were found to be quite different, in spite of the enzymes in the final step of the peroxisomal fatty acid β-oxidation system.

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