cDNA cloning and characterization of a constitutively expressed isoform of the human peroxin Pex11p

Biochem Biophys Res Commun. 1998 Nov 18;252(2):529-33. doi: 10.1006/bbrc.1998.9684.

Abstract

We cloned a human cDNA encoding an isoform of the peroxin Pex11p, termed Pex11pbeta, by screening of human liver cDNA library using as a probe human EST-derived, approximately 300 bp-long nucleotides showing homology to PEX11 from Candida boidinii and Saccharomyces cerevisiae. PEX11beta encoded a protein comprising 259 amino acids, with two putative transmembrane segments, showing approximately 40% identity to inducible Pex11palpha, at the amino acid sequence level. Pex11pbeta was found to be a peroxisomal protein, as assessed by colocalization with acyl-CoA oxidase, an enzyme catalyzing the first step of peroxisomal beta-oxidation system, in Pex11pbeta-expressing Chinese hamster ovary cells. PEX11beta was not induced in rats by treatment of clofibrate, a peroxisome proliferator, in contrast to PEX11alpha.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • CHO Cells
  • Cloning, Molecular
  • Cricetinae
  • DNA Primers / genetics
  • DNA, Complementary / genetics*
  • Gene Expression
  • Humans
  • Membrane Proteins / genetics*
  • Membrane Proteins / metabolism
  • Microbodies / metabolism*
  • Molecular Sequence Data
  • Peroxins
  • Polymerase Chain Reaction
  • Rats
  • Sequence Homology, Amino Acid
  • Subcellular Fractions / metabolism

Substances

  • DNA Primers
  • DNA, Complementary
  • Membrane Proteins
  • PEX11A protein, human
  • PEX11B protein, human
  • Peroxins
  • Pex11a protein, rat

Associated data

  • GENBANK/AB018080