Phosphorylation of cytochrome b6 by the LHC II kinase associated with the cytochrome complex
- 17 February 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 298 (1), 33-35
- https://doi.org/10.1016/0014-5793(92)80016-a
Abstract
The cytochrome b6 polypeptide present in cytochrome b6/| preparations from spinach thylakoids is phosphorylated concomitantly with the autophosphorylation of the 64 kDa polypeptide identified as the redox-controlled LHCII kinase. The N-terminal sequence of the 64 kDa kinase and sequence analysis of cytochrome b6 indicate the existence of putative phosphorylation sites in both proteinsKeywords
This publication has 14 references indexed in Scilit:
- Lateral redistribution of cytochrome b6/f complexes along thylakoid membranes upon state transitions.Proceedings of the National Academy of Sciences of the United States of America, 1991
- Protein Phosphorylation in Green Plant ChloroplastsAnnual Review of Plant Physiology and Plant Molecular Biology, 1991
- The ‘positive‐inside rule’ applies to thylakoid membrane proteinsFEBS Letters, 1991
- Use of synthetic peptides to study the substrate specificity of a thylakoid protein kinaseFEBS Letters, 1989
- A new siliconized‐glass fiber as support for protein‐chemical analysis of electroblotted proteins.European Journal of Biochemistry, 1988
- Chloroplast thylakoid protein phosphorylation is influenced by mutations in the cytochrome bf complexBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1988
- Chloroplast phosphoproteins: Phosphorylation of a 12-kDa stromal protein by the redox-controlled kinase of thylakoid membranesArchives of Biochemistry and Biophysics, 1987
- Protein kinases of the thylakoid membrane.Journal of Biological Chemistry, 1986
- Purification and characterization of a membrane-bound protein kinase from spinach thylakoids.Journal of Biological Chemistry, 1986
- Sequence homology and structural similarity between cytochrome b of mitochondrial complex III and the chloroplast b6-f complex: position of the cytochrome b hemes in the membrane.Proceedings of the National Academy of Sciences, 1984