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Molecular recognition in thylakoid structure and function

Allen, J.F. and Forsberg, Jens LU (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)
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author
organization
publishing date
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
2008-06-23 14:42:54
date last changed
2018-08-12 03:25:51
@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},
  volume       = {6},
  year         = {2001},
}