Nucleotide sequence of a cDNA coding for the NADPH-protochlorophyllide oxidoreductase (PCR) of barley (Hordeum vulgare L.) and its expression in Escherichia coli

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The primary structure of the NADPH-protochlorophyllide oxidoreductase of barley has been deduced from the nucleotide sequence of a cloned full-length cDNA. This cDNA hybridizes to a 1.7 kb RNA whose steady-state level in dark-grown seedlings is drastically reduced upon illumination. The predicted amino acid sequence (388 residues in length) includes a transit peptide of 74 amino acids whose end point has been delimited by sequencing the N-terminus of the mature protein. Expression of the cDNA in Escherichia coli leads to the synthesis of an enzymatically active precursor of the NADPH-protochlorophyllide oxidoreductase. Activity of this protein in bacterial lysates is completely dependent on the presence of NADPH and protochlorophyllide and requires light.

Original languageEnglish
JournalMGG Molecular & General Genetics
Volume217
Issue number2-3
Pages (from-to)355-361
Number of pages7
ISSN0026-8925
DOIs
Publication statusPublished - 1 Jun 1989

    Research areas

  • Barley, cDNA sequence, Light regulation, NADPH-protochlorophyllide oxidoreductase, Transit peptide

ID: 204471569