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 language | English |
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Journal | MGG Molecular & General Genetics |
Volume | 217 |
Issue number | 2-3 |
Pages (from-to) | 355-361 |
Number of pages | 7 |
ISSN | 0026-8925 |
DOIs | |
Publication status | Published - 1 Jun 1989 |
- Barley, cDNA sequence, Light regulation, NADPH-protochlorophyllide oxidoreductase, Transit peptide
Research areas
ID: 204471569