Molecular and General Genetics MGG

, Volume 233, Issue 1, pp 122–128

Isolation and characterization of a cDNA fromCuphea lanceolata encoding a β-ketoacyl-ACP reductase

  • Barbara Klein
  • Katharina Pawlowski
  • Christa Höricke-Grandpierre
  • Jeff Schell
  • Reinhard Töpfer
Article

DOI: 10.1007/BF00587569

Cite this article as:
Klein, B., Pawlowski, K., Höricke-Grandpierre, C. et al. Molec. Gen. Genet. (1992) 233: 122. doi:10.1007/BF00587569

Summary

A cDNA encoding β-ketoacyl-ACP reductase (EC 1.1.1.100), an integral part of the fatty acid synthase type II, was cloned fromCuphea lanceolata. This cDNA of 1276 by codes for a polypeptide of 320 amino acids with 63 N-terminal residues presumably representing a transit peptide and 257 residues corresponding to the mature protein of 27 kDa. The encoded protein shows strong homology with the amino-terminal sequence and two tryptic peptides from avocado mesocarp β-ketoacyl-ACP reductase, and its total amino acid composition is highly similar to those of the β-ketoacyl-ACP reductases of avocado and spinach. Amino acid sequence homologies to polyketide synthase, β-ketoreductases and short-chain alcohol dehydrogenases are discussed. An engineered fusion protein lacking most of the transit peptide, which was produced inEscherichia coli, was isolated and proved to possess β-ketoacyl-ACP reductase activity. Hybridization studies revealed that inC. lanceolata β-ketoacyl-ACP reductase is encoded by a small family of at least two genes and that members of this family are expressed in roots, leaves, flowers and seeds.

Key words

Cuphea Fatty acid synthase β-KetoacylACP reductase Polyketide synthase Short-chain alcohol dehydrogenase family 

Copyright information

© Springer-Verlag 1992

Authors and Affiliations

  • Barbara Klein
    • 1
  • Katharina Pawlowski
    • 1
  • Christa Höricke-Grandpierre
    • 1
  • Jeff Schell
    • 1
  • Reinhard Töpfer
    • 1
  1. 1.Max-Planck-Institut für ZüchtungsforschungKöln 30Germany

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