Isolation and characterization of the cDNA for pea chloroplast SecA. Evolutionary conservation of the bacterial-type SecA-dependent protein transport within chloroplasts

FEBS Lett. 1995 May 15;364(3):305-8. doi: 10.1016/0014-5793(95)00415-6.

Abstract

We report here the isolation of the cDNA for pea chloroplast SecA. Pea SecA encodes a polypeptide of 1,011 amino acids and shows high sequence similarity with cyanobacterial SecA. Pea SecA was synthesized as a larger precursor and was imported into isolated chloroplasts in vitro. The purified pea SecA, which was expressed in Escherichia coli cells, stimulated the in vitro import of the 33 kDa protein of the oxygen-evolving complex into thylakoids. These results indicate that higher plant chloroplasts contain a bacterial-type SecA protein-dependent system for the intraorganellar protein transport into thylakoids.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / genetics*
  • Adenosine Triphosphatases / pharmacology
  • Amino Acid Sequence
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / pharmacology
  • Base Sequence
  • Biological Evolution*
  • Biological Transport / drug effects
  • Chloroplasts / chemistry*
  • Conserved Sequence
  • Cyanobacteria / chemistry
  • DNA, Complementary / chemistry
  • DNA, Complementary / isolation & purification*
  • Escherichia coli / genetics
  • Escherichia coli Proteins*
  • Fabaceae / genetics*
  • Membrane Transport Proteins*
  • Molecular Sequence Data
  • Molecular Weight
  • Plant Proteins / metabolism*
  • Plants, Medicinal*
  • Polymerase Chain Reaction
  • Recombinant Proteins
  • SEC Translocation Channels
  • SecA Proteins
  • Sequence Homology

Substances

  • Bacterial Proteins
  • DNA, Complementary
  • Escherichia coli Proteins
  • Membrane Transport Proteins
  • Plant Proteins
  • Recombinant Proteins
  • SEC Translocation Channels
  • Adenosine Triphosphatases
  • SecA Proteins

Associated data

  • GENBANK/X82404