Nucleotide sequence of a cDNA clone encoding a Caenorhabditis elegans homolog of mammalian alkyl-dihydroxyacetonephosphate synthase: evolutionary switching of peroxisomal targeting signals

E C de Vet, H C Prinsen, H van den Bosch

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

The nucleotide sequence is reported of a cDNA clone encoding a Caenorhabditis elegans homolog of guinea pig and human alkyl-dihydroxyacetonephosphate synthase. The open reading frame encodes a protein of 597 amino acids which shows extensive homology with the mammalian enzymes (52% identical and about 76% similar in the overlapping region). In contrast to the mammalian enzymes, which carry a consensus peroxisomal targeting signal type 2 in a cleavable N-terminal presequence, this Caenorhabditis elegans homolog carries a consensus peroxisomal targeting signal type 1 (CKL) at its C-terminus. Expression of this protein in an in vitro transcription/translation system yielded a 65 kDa protein. Recombinant aenorhabditis elegans alkyl-DHAP synthase expressed in the yeast Pichia pastoris was enzymatically active.

Original languageEnglish
Pages (from-to)277-81
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume242
Issue number2
DOIs
Publication statusPublished - 14 Jan 1998

Keywords

  • Alkyl and Aryl Transferases
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Caenorhabditis elegans
  • Cloning, Molecular
  • Electrophoresis, Polyacrylamide Gel
  • Gene Expression Regulation, Fungal
  • Helminth Proteins
  • Microbodies
  • Molecular Sequence Data
  • Pichia
  • Protein Biosynthesis
  • Protein Sorting Signals
  • Recombinant Proteins
  • Sequence Alignment
  • Sequence Analysis, DNA
  • Transcription, Genetic

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