Protein tyrosine phosphorylation in the transition to light state 2 of chloroplast thylakoids
(2001) In Photosynthesis Research 68(1). p.71-79- Abstract
- Redox dependent protein phosphorylation in chloroplast thylakoids regulates distribution of excitation energy between the two photosystems of photosynthesis, PS I and PS II. Several thylakoid phosphoproteins are known to be phosphorylated on N-terminal threonine residues exposed to the chloroplast stroma. Phosphorylation of light harvesting complex II (LHC II) on Thr-6 is thought to account for redistribution of light energy from PS II to PS I during the transition to light state 2. Here, we present evidence that a protein tyrosine kinase activity is required for the transition to light state 2. With an immunological approach using antibodies directed specifically towards either phospho-tyrosine or phospho-threonine, we observed that LHC... (More)
- Redox dependent protein phosphorylation in chloroplast thylakoids regulates distribution of excitation energy between the two photosystems of photosynthesis, PS I and PS II. Several thylakoid phosphoproteins are known to be phosphorylated on N-terminal threonine residues exposed to the chloroplast stroma. Phosphorylation of light harvesting complex II (LHC II) on Thr-6 is thought to account for redistribution of light energy from PS II to PS I during the transition to light state 2. Here, we present evidence that a protein tyrosine kinase activity is required for the transition to light state 2. With an immunological approach using antibodies directed specifically towards either phospho-tyrosine or phospho-threonine, we observed that LHC II became phosphorylated on both tyrosine and threonine residues. The specific protein tyrosine kinase inhibitor genistein, at concentrations causing no direct effect on threonine kinase activity, was found to prevent tyrosine phosphorylation of LHC II, the transition to light state 2, and associated threonine phosphorylation of LHC II. Possible reasons for an involvement of tyrosine phosphorylation in light state transitions are proposed and discussed. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1118928
- author
- Forsberg, Jens LU and Allen, John LU
- organization
- publishing date
- 2001
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Photosynthesis Research
- volume
- 68
- issue
- 1
- pages
- 71 - 79
- publisher
- Springer
- external identifiers
-
- wos:000170974200006
- scopus:0034787606
- ISSN
- 0166-8595
- language
- English
- LU publication?
- yes
- id
- 12989989-baab-4d6a-b251-4683d745c12f (old id 1118928)
- date added to LUP
- 2016-04-01 16:49:21
- date last changed
- 2022-01-28 22:23:13
@article{12989989-baab-4d6a-b251-4683d745c12f,
abstract = {{Redox dependent protein phosphorylation in chloroplast thylakoids regulates distribution of excitation energy between the two photosystems of photosynthesis, PS I and PS II. Several thylakoid phosphoproteins are known to be phosphorylated on N-terminal threonine residues exposed to the chloroplast stroma. Phosphorylation of light harvesting complex II (LHC II) on Thr-6 is thought to account for redistribution of light energy from PS II to PS I during the transition to light state 2. Here, we present evidence that a protein tyrosine kinase activity is required for the transition to light state 2. With an immunological approach using antibodies directed specifically towards either phospho-tyrosine or phospho-threonine, we observed that LHC II became phosphorylated on both tyrosine and threonine residues. The specific protein tyrosine kinase inhibitor genistein, at concentrations causing no direct effect on threonine kinase activity, was found to prevent tyrosine phosphorylation of LHC II, the transition to light state 2, and associated threonine phosphorylation of LHC II. Possible reasons for an involvement of tyrosine phosphorylation in light state transitions are proposed and discussed.}},
author = {{Forsberg, Jens and Allen, John}},
issn = {{0166-8595}},
language = {{eng}},
number = {{1}},
pages = {{71--79}},
publisher = {{Springer}},
series = {{Photosynthesis Research}},
title = {{Protein tyrosine phosphorylation in the transition to light state 2 of chloroplast thylakoids}},
volume = {{68}},
year = {{2001}},
}