Open Access3‐Hydroxy‐3‐methylglutaryl‐coenzyme‐A synthase from Blattella germanica
Author(s) -
MARTÍNEZGONZÁLEZ José,
BUESA Carlos,
PIULACHS MaríaDolos,
BELLÉS Xavier,
HEGARDT Fausto G.
Publication year - 1993
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1993.tb18295.x
Subject(s) - biology , complementary dna , atp synthase , coenzyme a , microbiology and biotechnology , farnesyl diphosphate synthase , rapid amplification of cdna ends , biochemistry , reductase , gene , enzyme , molecular cloning
Insects do not synthezise cholesterol; the 3‐hydroxy‐3‐methylglutaryl‐coenzyme‐A (HMG‐CoA) produced by HMG‐CoA synthase is transformed to mevalonate by HMG‐CoA reductase for the production of non‐sterol isoprenoids, which are essential for growth and differentiation. To understand the regulation and developmental role of HMG‐CoA synthase, we have cloned a 1658 bp cDNA that encompasses the entire transcription unit of the HMG‐CoA synthase gene from the cockroach Blattella germanica . This cDNA clone was isolated using as a probe a partial cDNA of B. germanica HMG‐CoA synthase, amplified using the polymerase chain reaction. Analysis of the nucleotide sequence reveals that the cDNA encodes a polypeptide of 453 amino acids ( M r 50338) that is similar to vertebrate HMG‐CoA synthase (74–76% conserved residues). The B. germanica cDNA has been expressed as a fusion protein in Escherichia coli and exhibits HMG‐CoA synthase activity. The HMG‐CoA synthase transcript was differentially expressed throughout B. germanica development. Analysis of RNA samples from different adult female tissues shows high HMG‐CoA synthase mRNA levels in the ovary and lower levels in brain and muscle.