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Reishi, Lingzhi · 2008 · Journal Article

Medium relevance

Cloning and Characterization of a Gene Encoding HMG-CoA Reductase from Ganoderma lucidum and Its Functional Identification in Yeast

Ganoderma lucidum

SpeciesReishi, Lingzhi
JournalBioscience, Biotechnology, and Biochemistry
Year2008

Key points

  • A gene encoding 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGR) was isolated from a triterpene-producing fungus, Ganoderma lucidum (Reishi or Lingzhi)
  • This report provides the complete nucleotide sequence of the full-length cDNA encoding HMGR and its genomic DNA sequence
  • The cDNA of the HMGR (GenBank Accession no., EU263989) was found to contain an open reading frame (ORF) of 3,681 bp encoding a 1,226-amino-acid polypeptide, whereas the HMGR genomic DNA sequence (GenBank Accession no., EU263990) consisted of 4,262 bp and contained seven exons and six introns
  • The deduced amino acid sequence of G. lucidum HMGR showed significant homology to the known HMGRs from Ustilago maydis and Cryptococcus neoformans, and contained four conserved domains
  • Gene expression analysis showed that the expression level was relatively low in mycelia incubated for 10, 12, and 14 d, and reached the highest level in the primordia
  • Functional complementation of Gl-HMGR in a HMGR-deficient mutant yeast strain indicated that the cloned cDNA encoded a HMG-CoA reductase

From the paper

Abstract

A gene encoding 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGR) was isolated from a triterpene-producing fungus, Ganoderma lucidum (Reishi or Lingzhi). This report provides the complete nucleotide sequence of the full-length cDNA encoding HMGR and its genomic DNA sequence. The cDNA of the HMGR (GenBank Accession no., EU263989) was found to contain an open reading frame (ORF) of 3,681 bp encoding a 1,226-amino-acid polypeptide, whereas the HMGR genomic DNA sequence (GenBank Accession no., EU263990) consisted of 4,262 bp and contained seven exons and six introns. The deduced amino acid sequence of G. lucidum HMGR showed significant homology to the known HMGRs from Ustilago maydis and Cryptococcus neoformans, and contained four conserved domains. Gene expression analysis showed that the expression level was relatively low in mycelia incubated for 10, 12, and 14 d, and reached the highest level in the primordia. Functional complementation of Gl-HMGR in a HMGR-deficient mutant yeast strain indicated that the cloned cDNA encoded a HMG-CoA reductase.

Citation

Chang-Hua SHANG Fen ZHU Na LI Xiang OU-YANG Liang SHI Ming-Wen ZHAO Yu-Xiang LI (2008). Cloning and Characterization of a Gene Encoding HMG-CoA Reductase from Ganoderma lucidum and Its Functional Identification in Yeast. Bioscience, Biotechnology, and Biochemistry https://doi.org/10.1271/bbb.80011

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