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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Nucleotide sequence of a cDNA coding for the NADPH-protochlorophyllide oxidoreductase (PCR) of barley (Hordeum vulgare L.) and its expression in Escherichia coli. / Schulz, Rüdiger; Steinmüller, Klaus; Klaas, Manfred; Forreiter, Christoph; Rasmussen, Sören; Hiller, Claudia; Apel, Klaus.
In: MGG Molecular & General Genetics, Vol. 217, No. 2-3, 01.06.1989, p. 355-361.Research output: Contribution to journal › Journal article › Research › peer-review
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T1 - Nucleotide sequence of a cDNA coding for the NADPH-protochlorophyllide oxidoreductase (PCR) of barley (Hordeum vulgare L.) and its expression in Escherichia coli
AU - Schulz, Rüdiger
AU - Steinmüller, Klaus
AU - Klaas, Manfred
AU - Forreiter, Christoph
AU - Rasmussen, Sören
AU - Hiller, Claudia
AU - Apel, Klaus
PY - 1989/6/1
Y1 - 1989/6/1
N2 - 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.
AB - 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.
KW - Barley
KW - cDNA sequence
KW - Light regulation
KW - NADPH-protochlorophyllide oxidoreductase
KW - Transit peptide
UR - http://www.scopus.com/inward/record.url?scp=0024676061&partnerID=8YFLogxK
U2 - 10.1007/BF02464904
DO - 10.1007/BF02464904
M3 - Journal article
C2 - 2671659
AN - SCOPUS:0024676061
VL - 217
SP - 355
EP - 361
JO - Molecular General Genetics
JF - Molecular General Genetics
SN - 0026-8925
IS - 2-3
ER -
ID: 204471569