Cloning and regulation of rat and Xenopus laevis hepatic 3-hydroxy-3-methylglutaryl Coenzyme A reductase

The cDNAs coding for rat and Xenopus laevis 3-hydroxy-3-methylglutaryl Coenzyme A (HMG-CoA) reductase have been cloned and sequenced. The rat liver HMG-CoA reductase cDNA clone contains one open reading frame coding for 887 amino acids. Its 106 nucleotide long 5$\sp\prime$-noncoding region contains no additional start codons. It does not contain a poly(A) tract at the 3$\sp\prime$ end. The Xenopus liver HMG-CoA reductase cDNA encodes 883 amino acids, and contains 114 nucleotides at the 5$\sp\prime$-untranslated region. Primer extension analysis and RNA sequencing indicate that HMG-CoA reductase mRNAs in both animals are transcribed from multiple initiation sites. Rat reductase RNA precursor, like the human precursor, is processed at a single donor site to excise the first intron, producing only one class of mRNA equivalent to hamster class I reductase mRNA. Comparison of the amino acid sequences of the mammalian and amphibian HMG-CoA reductases reveals a high degree of amino acid sequence conservation. The seven membrane spanning domains exhibit the highest amino acid sequence similarity, while the linker region displays the lowest level of amino acid homology.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Chen, Hangjiong

Contributors dc:contributor

• Shapiro, David J.

• Biology, Molecular
• Chemistry, Biochemistry

Statement dc:rights

• Copyright 1990 Chen, Hangjiong

Language dc:language

eng

Identifier

AAI9021661
(UMI)AAI9021661

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/20680