Expression of the barley psbA gene inEscherichia coliyields a functional in vitro photosystem II protein D1
- 11 July 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 348 (2) , 153-157
- https://doi.org/10.1016/0014-5793(94)00586-9
Abstract
The barley chloroplast psbA gene encoding D1 protein, one of the main photosystem II components, has been over-expressed in E. coli cells. The existance of two in vivo expression products, a protein with M r about 33.5 kDa, corresponding to the full-length precursor of the 32 kDa D1 mature form, and a truncated 29 kDa polypeptide was revealed. A modified D1 protein containing six histidine residues at the carboxy-terminus was also obtained. After isolation and renaturation, the ability of the recombinant D1 protein to bind atrazine and pigments from barley thylakoids was demonstrated.Keywords
This publication has 10 references indexed in Scilit:
- Dipentafluorophenyl carbonate—a reagent for the synthesis of oligonucleotides and their conjugatesNucleic Acids Research, 1993
- Expression vectors for streptavidin-containing chimeric proteinsBiochemical and Biophysical Research Communications, 1991
- Reconstitution of pigment-containing complexes from light-harvesting chlorophyll a/b-binding protein overexpressed inEscherichia coliPlanta, 1990
- Nucleotide sequence of the barley chloroplast psbA gene for the QBprotein of photosystem IINucleic Acids Research, 1988
- Isolation of a photosystem II reaction center consisting of D-1 and D-2 polypeptides and cytochrome b -559Proceedings of the National Academy of Sciences, 1987
- The amino terminal region delimited by Met1 and Met37 is an integral part of the 32 kDa herbicide binding proteinPlant Molecular Biology, 1987
- In vitroexpression and characterization of the translation start site of thepsbA gene product (QBprotein) from higher plantsNucleic Acids Research, 1984
- Nucleotide sequence of the gene for the M r 32,000 thylakoid membrane protein from Spinacia oleracea and Nicotiana debneyi predicts a totally conserved primary translation product of M r 38,950Proceedings of the National Academy of Sciences, 1982
- Some preparative and analytical applications of triazine dyesInternational Journal of Biochemistry, 1981
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970