Molecular cloning of mouse alcohol dehydrogenase-b2 cDNA: Nucleotide sequences of the class III ADH genes evolve slowly even for silent substitutions

Man Wook Hur, Wei Hsien Ho, Celeste J. Brown, David Goldman, Howard Edenberg

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

We have cloned and sequenced a cDNA encoding the mouse class III alcohol dehydrogenase, Adh-B2. Adh-B2 mRNA is detectable in all the mouse tissues tested. Class III ADHs are highly conserved: the deduced ammo acid sequence of the mouse Adh-B2 is 91 to 97% identical to the human, horse and rat liver enzymes. The mouse Adh-B2 cDNA is 87% identical in nucleotide sequence to the human χADH cDNA. Previously, a slower rate of evolutionary divergence of the amino acid sequences of class III ADH proteins was detected and ascribed to functional constraints upon the protein. Our analysis of the nucleotide sequences demonstrates that this cannot be the entire explanation, since the rate of silent (synonymous) nucleotide substitutions is also lower in the class III ADHs than in the class I ADHs.

Original languageEnglish
Pages (from-to)167-175
Number of pages9
JournalMitochondrial DNA
Volume3
Issue number3
DOIs
StatePublished - 1992

Fingerprint

Alcohol Dehydrogenase
Cloning
Molecular Cloning
Substitution reactions
Nucleotides
Complementary DNA
Genes
Liver
Rats
Proteins
Tissue
Horses
Amino Acids
Amino Acid Sequence
Messenger RNA
Acids
Enzymes

Keywords

  • Alcohol dehydrogenase
  • CDNA
  • Evolution
  • Formaldehyde dehydrogenase
  • Silent substitutions

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology
  • Biochemistry
  • Endocrinology

Cite this

Molecular cloning of mouse alcohol dehydrogenase-b2 cDNA : Nucleotide sequences of the class III ADH genes evolve slowly even for silent substitutions. / Hur, Man Wook; Ho, Wei Hsien; Brown, Celeste J.; Goldman, David; Edenberg, Howard.

In: Mitochondrial DNA, Vol. 3, No. 3, 1992, p. 167-175.

Research output: Contribution to journalArticle

@article{6c1c63ea71ad454b8ff8f92086ddcde0,
title = "Molecular cloning of mouse alcohol dehydrogenase-b2 cDNA: Nucleotide sequences of the class III ADH genes evolve slowly even for silent substitutions",
abstract = "We have cloned and sequenced a cDNA encoding the mouse class III alcohol dehydrogenase, Adh-B2. Adh-B2 mRNA is detectable in all the mouse tissues tested. Class III ADHs are highly conserved: the deduced ammo acid sequence of the mouse Adh-B2 is 91 to 97{\%} identical to the human, horse and rat liver enzymes. The mouse Adh-B2 cDNA is 87{\%} identical in nucleotide sequence to the human χADH cDNA. Previously, a slower rate of evolutionary divergence of the amino acid sequences of class III ADH proteins was detected and ascribed to functional constraints upon the protein. Our analysis of the nucleotide sequences demonstrates that this cannot be the entire explanation, since the rate of silent (synonymous) nucleotide substitutions is also lower in the class III ADHs than in the class I ADHs.",
keywords = "Alcohol dehydrogenase, CDNA, Evolution, Formaldehyde dehydrogenase, Silent substitutions",
author = "Hur, {Man Wook} and Ho, {Wei Hsien} and Brown, {Celeste J.} and David Goldman and Howard Edenberg",
year = "1992",
doi = "10.3109/10425179209034012",
language = "English",
volume = "3",
pages = "167--175",
journal = "DNA Sequence - Journal of DNA Sequencing and Mapping",
issn = "1940-1736",
publisher = "Informa Healthcare",
number = "3",

}

TY - JOUR

T1 - Molecular cloning of mouse alcohol dehydrogenase-b2 cDNA

T2 - Nucleotide sequences of the class III ADH genes evolve slowly even for silent substitutions

AU - Hur, Man Wook

AU - Ho, Wei Hsien

AU - Brown, Celeste J.

AU - Goldman, David

AU - Edenberg, Howard

PY - 1992

Y1 - 1992

N2 - We have cloned and sequenced a cDNA encoding the mouse class III alcohol dehydrogenase, Adh-B2. Adh-B2 mRNA is detectable in all the mouse tissues tested. Class III ADHs are highly conserved: the deduced ammo acid sequence of the mouse Adh-B2 is 91 to 97% identical to the human, horse and rat liver enzymes. The mouse Adh-B2 cDNA is 87% identical in nucleotide sequence to the human χADH cDNA. Previously, a slower rate of evolutionary divergence of the amino acid sequences of class III ADH proteins was detected and ascribed to functional constraints upon the protein. Our analysis of the nucleotide sequences demonstrates that this cannot be the entire explanation, since the rate of silent (synonymous) nucleotide substitutions is also lower in the class III ADHs than in the class I ADHs.

AB - We have cloned and sequenced a cDNA encoding the mouse class III alcohol dehydrogenase, Adh-B2. Adh-B2 mRNA is detectable in all the mouse tissues tested. Class III ADHs are highly conserved: the deduced ammo acid sequence of the mouse Adh-B2 is 91 to 97% identical to the human, horse and rat liver enzymes. The mouse Adh-B2 cDNA is 87% identical in nucleotide sequence to the human χADH cDNA. Previously, a slower rate of evolutionary divergence of the amino acid sequences of class III ADH proteins was detected and ascribed to functional constraints upon the protein. Our analysis of the nucleotide sequences demonstrates that this cannot be the entire explanation, since the rate of silent (synonymous) nucleotide substitutions is also lower in the class III ADHs than in the class I ADHs.

KW - Alcohol dehydrogenase

KW - CDNA

KW - Evolution

KW - Formaldehyde dehydrogenase

KW - Silent substitutions

UR - http://www.scopus.com/inward/record.url?scp=0027013538&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027013538&partnerID=8YFLogxK

U2 - 10.3109/10425179209034012

DO - 10.3109/10425179209034012

M3 - Article

C2 - 1472709

AN - SCOPUS:0027013538

VL - 3

SP - 167

EP - 175

JO - DNA Sequence - Journal of DNA Sequencing and Mapping

JF - DNA Sequence - Journal of DNA Sequencing and Mapping

SN - 1940-1736

IS - 3

ER -