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Molecular cloning and structural analysis of 3‐hydroxy‐3‐methylglutaryl coenzyme A reductase of the moth Agrotis ipsilon
Author(s) -
Duportets L.,
Belles X.,
Rossignol F.,
Couillaud F.
Publication year - 2000
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1046/j.1365-2583.2000.00200.x
Subject(s) - biology , reductase , eukaryote , agrotis ipsilon , biochemistry , coenzyme a , thiolase , genetics , enzyme , botany , gene , lepidoptera genitalia , peroxisome , genome , noctuidae , cutworm
The enzyme 3‐hydroxy‐3‐methylglutaryl coenzyme A (HMG‐CoA) reductase, which plays a key role in isoprenoid biosynthesis, catalyses the synthesis of mevalonate from HMG‐CoA. Insects do not synthesize cholesterol de novo , rather mevalonate derivatives lead to non‐sterol isoprenoids which are essential for development and reproduction. In this paper, we describe an HMG‐CoA reductase of the moth Agrotis ipsilon and we report its expression in fat body, ovary, muscle, brain and corpora allata tissues of adult specimens. The analysis of the cDNA reveals that it encodes a polypeptide of 833 amino acids ( M r = 89785). Alignments of this HMG‐CoA reductase from A. ipsilon with the homologous sequences of other eukaryotes shows a high degree of conservation in all species studied. Parsimony analysis based on these alignments produced dendrograms congruent with the current systematic schemes. This suggests that, during eukaryote evolution, HMG‐CoA reductase diversified in parallel with taxonomic splitting.