Identification and characterization of novel cytochrome P450 genes from the white-rot basidiomycete, Coriolus versicolor

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Abstract

Using a reverse-transcription polymerase chain reaction (RT-PCR) technique, cytochrome P450 genes were cloned from the lignin-degrading basidiomycete, Coriolus versicolor. One possible P450 gene was identified, which consisted of 1,672 nucleotides and a poly(A) tail and encoded a deduced protein containing 449 amino acids. The deduced amino acid sequence revealed the presence of the P450 heme-binding motif, strongly suggesting that this protein belongs to the P450 superfamily, then designated CYP512A1. The deduced protein showed sequential similarity to other known P450s from several micro-organisms, such as Aspergillus terreus, Gibberella fujikuroi, and Neurospora crassa, with 30-35% identity. Since the identity of the amino acid sequence was less than 40% with any other P450s, this protein was suggested to be the first member of a new family of cytochrome P450. In addition, a differential display RT-PCR analysis showed the expression of the other P450 genes, which were up-regulated by the addition of dibenzothiophene and 4-methyldibenzothiophene-5-oxide. Using the 5′ rapid amplification of cDNA ends method, a 520-nucleotide sequence, including the P450 motif-coding region, was determined for one clone. The deduced protein showed high similarity to CYP512A1 but less than 40% identity with P450s from other organisms. A chemical stress-responsive expression of P450 is suggested for the first time in basidiomycetes.

Original languageEnglish
Pages (from-to)97-105
Number of pages9
JournalApplied Microbiology and Biotechnology
Volume58
Issue number1
DOIs
Publication statusPublished - Feb 23 2002

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Basidiomycota
Cytochrome P-450 Enzyme System
Genes
Proteins
Reverse Transcription
Amino Acid Sequence
Gibberella
Polymerase Chain Reaction
Neurospora crassa
Lignin
Aspergillus
Heme
Oxides
Nucleotides
Complementary DNA
Clone Cells
Amino Acids
Messenger RNA

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Applied Microbiology and Biotechnology

Cite this

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title = "Identification and characterization of novel cytochrome P450 genes from the white-rot basidiomycete, Coriolus versicolor",
abstract = "Using a reverse-transcription polymerase chain reaction (RT-PCR) technique, cytochrome P450 genes were cloned from the lignin-degrading basidiomycete, Coriolus versicolor. One possible P450 gene was identified, which consisted of 1,672 nucleotides and a poly(A) tail and encoded a deduced protein containing 449 amino acids. The deduced amino acid sequence revealed the presence of the P450 heme-binding motif, strongly suggesting that this protein belongs to the P450 superfamily, then designated CYP512A1. The deduced protein showed sequential similarity to other known P450s from several micro-organisms, such as Aspergillus terreus, Gibberella fujikuroi, and Neurospora crassa, with 30-35{\%} identity. Since the identity of the amino acid sequence was less than 40{\%} with any other P450s, this protein was suggested to be the first member of a new family of cytochrome P450. In addition, a differential display RT-PCR analysis showed the expression of the other P450 genes, which were up-regulated by the addition of dibenzothiophene and 4-methyldibenzothiophene-5-oxide. Using the 5′ rapid amplification of cDNA ends method, a 520-nucleotide sequence, including the P450 motif-coding region, was determined for one clone. The deduced protein showed high similarity to CYP512A1 but less than 40{\%} identity with P450s from other organisms. A chemical stress-responsive expression of P450 is suggested for the first time in basidiomycetes.",
author = "Hirofumi Ichinose and Hiroyuki Wariishi and H. Tanaka",
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N2 - Using a reverse-transcription polymerase chain reaction (RT-PCR) technique, cytochrome P450 genes were cloned from the lignin-degrading basidiomycete, Coriolus versicolor. One possible P450 gene was identified, which consisted of 1,672 nucleotides and a poly(A) tail and encoded a deduced protein containing 449 amino acids. The deduced amino acid sequence revealed the presence of the P450 heme-binding motif, strongly suggesting that this protein belongs to the P450 superfamily, then designated CYP512A1. The deduced protein showed sequential similarity to other known P450s from several micro-organisms, such as Aspergillus terreus, Gibberella fujikuroi, and Neurospora crassa, with 30-35% identity. Since the identity of the amino acid sequence was less than 40% with any other P450s, this protein was suggested to be the first member of a new family of cytochrome P450. In addition, a differential display RT-PCR analysis showed the expression of the other P450 genes, which were up-regulated by the addition of dibenzothiophene and 4-methyldibenzothiophene-5-oxide. Using the 5′ rapid amplification of cDNA ends method, a 520-nucleotide sequence, including the P450 motif-coding region, was determined for one clone. The deduced protein showed high similarity to CYP512A1 but less than 40% identity with P450s from other organisms. A chemical stress-responsive expression of P450 is suggested for the first time in basidiomycetes.

AB - Using a reverse-transcription polymerase chain reaction (RT-PCR) technique, cytochrome P450 genes were cloned from the lignin-degrading basidiomycete, Coriolus versicolor. One possible P450 gene was identified, which consisted of 1,672 nucleotides and a poly(A) tail and encoded a deduced protein containing 449 amino acids. The deduced amino acid sequence revealed the presence of the P450 heme-binding motif, strongly suggesting that this protein belongs to the P450 superfamily, then designated CYP512A1. The deduced protein showed sequential similarity to other known P450s from several micro-organisms, such as Aspergillus terreus, Gibberella fujikuroi, and Neurospora crassa, with 30-35% identity. Since the identity of the amino acid sequence was less than 40% with any other P450s, this protein was suggested to be the first member of a new family of cytochrome P450. In addition, a differential display RT-PCR analysis showed the expression of the other P450 genes, which were up-regulated by the addition of dibenzothiophene and 4-methyldibenzothiophene-5-oxide. Using the 5′ rapid amplification of cDNA ends method, a 520-nucleotide sequence, including the P450 motif-coding region, was determined for one clone. The deduced protein showed high similarity to CYP512A1 but less than 40% identity with P450s from other organisms. A chemical stress-responsive expression of P450 is suggested for the first time in basidiomycetes.

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