Molecular recognition in thylakoid structure and function
(2001) In Trends in Plant Science 6(7). p.317-326- Abstract
- In photosynthesis, light-harvesting chlorophyll molecules are shunted between photosystems by phosphorylation of the protein to which they are bound, An anchor for the phosphorylated chlorophyll-protein complex has now been identified in the reaction centre of chloroplast photosystem I. This finding supports the idea that molecular recognition, not membrane surface charge, governs the architecture of the chloroplast thylakoid membrane. We describe a model for the chloroplast thylakoid membrane that is consistent with recent structural data that specify the relative dimensions of intrinsic protein complexes and their dispositions within the membrane. Control of molecular recognition accommodates membrane stacking, lateral heterogeneity and... (More)
- In photosynthesis, light-harvesting chlorophyll molecules are shunted between photosystems by phosphorylation of the protein to which they are bound, An anchor for the phosphorylated chlorophyll-protein complex has now been identified in the reaction centre of chloroplast photosystem I. This finding supports the idea that molecular recognition, not membrane surface charge, governs the architecture of the chloroplast thylakoid membrane. We describe a model for the chloroplast thylakoid membrane that is consistent with recent structural data that specify the relative dimensions of intrinsic protein complexes and their dispositions within the membrane. Control of molecular recognition accommodates membrane stacking, lateral heterogeneity and regulation of light-harvesting function by means of protein phosphorylation during state transitions - adaptations that compensate for selective excitation of photosystem I or photosystem II. High-resolution structural description of membrane protein-protein interactions is now required to understand thylakoid structure and regulation of photosynthesis. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1119090
- author
- Allen, J.F. and Forsberg, Jens LU
- organization
- publishing date
- 2001
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Trends in Plant Science
- volume
- 6
- issue
- 7
- pages
- 317 - 326
- publisher
- Elsevier
- external identifiers
-
- wos:000169811900012
- scopus:0035651544
- ISSN
- 1360-1385
- DOI
- 10.1016/S1360-1385(01)02010-6
- language
- English
- LU publication?
- yes
- id
- 05e8e7b1-6e77-4544-8d03-00c1869b9210 (old id 1119090)
- date added to LUP
- 2016-04-01 11:42:20
- date last changed
- 2022-02-10 20:14:03
@article{05e8e7b1-6e77-4544-8d03-00c1869b9210,
abstract = {{In photosynthesis, light-harvesting chlorophyll molecules are shunted between photosystems by phosphorylation of the protein to which they are bound, An anchor for the phosphorylated chlorophyll-protein complex has now been identified in the reaction centre of chloroplast photosystem I. This finding supports the idea that molecular recognition, not membrane surface charge, governs the architecture of the chloroplast thylakoid membrane. We describe a model for the chloroplast thylakoid membrane that is consistent with recent structural data that specify the relative dimensions of intrinsic protein complexes and their dispositions within the membrane. Control of molecular recognition accommodates membrane stacking, lateral heterogeneity and regulation of light-harvesting function by means of protein phosphorylation during state transitions - adaptations that compensate for selective excitation of photosystem I or photosystem II. High-resolution structural description of membrane protein-protein interactions is now required to understand thylakoid structure and regulation of photosynthesis.}},
author = {{Allen, J.F. and Forsberg, Jens}},
issn = {{1360-1385}},
language = {{eng}},
number = {{7}},
pages = {{317--326}},
publisher = {{Elsevier}},
series = {{Trends in Plant Science}},
title = {{Molecular recognition in thylakoid structure and function}},
url = {{http://dx.doi.org/10.1016/S1360-1385(01)02010-6}},
doi = {{10.1016/S1360-1385(01)02010-6}},
volume = {{6}},
year = {{2001}},
}