Pumpkin hydroxypyruvate reductases with and without a putative C-terminal signal for targeting to microbodies may be produced by alternative splicing

Plant Mol Biol. 1996 Jan;30(1):183-9. doi: 10.1007/BF00017813.


Two full-length cDNAs encoding hydroxypyruvate reductase were isolated from a cDNA library constructed with poly(A)+ RNA from pumpkin green cotyledons. One of the cDNAs, designated HPR1, encodes a polypeptide of 386 amino acids, while the other cDNA, HPR2 encodes a polypeptide of 381 amino acids. Although the nucleotide and deduced amino acid sequences of these cDNAs are almost identical, the deduced HPR1 protein contains Ser-Lys-Leu at its carboxy-terminal end, which is known as a microbody-targeting signal, while the deduced HPR2 protein does not. Analysis of genomic DNA strongly suggests that HPR1 and HPR2 are produced by alternative splicing.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Oxidoreductases / genetics*
  • Alternative Splicing
  • Amino Acid Sequence
  • Base Sequence
  • Biological Transport
  • Cell Compartmentation*
  • Cotyledon / enzymology
  • DNA, Complementary / genetics
  • Gene Library
  • Hydroxypyruvate Reductase
  • Isoenzymes / genetics*
  • Microbodies / enzymology*
  • Molecular Sequence Data
  • Plant Proteins / genetics
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Vegetables / enzymology
  • Vegetables / genetics*


  • DNA, Complementary
  • Isoenzymes
  • Plant Proteins
  • Alcohol Oxidoreductases
  • Hydroxypyruvate Reductase

Associated data

  • GENBANK/D49431
  • GENBANK/D49432
  • GENBANK/D49433