Advances in Photosynthesis Research pp 123-130 | Cite as
Lipid-protein Interactions in the Thylakoid Membranes of Higher Plant Chloroplasts
Abstract
The molecular organisation of the thylakoid membrane is usually described in terms of the fluid mosaic model. On this basis, the central matrix of the membrane is believed to consist of a fluid lipid bilayer. Membrane proteins are either attached to the surface of this bilayer by electrostatic forces or anchored within the bilayer by hydrophobic forces. A great deal of attention has been focussed on the spatial organisation of these protein components. Freeze-fracture studies have revealed the existence of large numbers of intra-membranous particles which can be characterised by their size, distribution between stromal and granal membranes, and the freeze-fracture faces with which they are associated (Staehelin et al. 1977; Arntzen 1978). Whilst there is still some debate regarding the origin of different groups of particles (Andersson, Anderson 1980), it is generally accepted that they reflect the presence of the chlorophyll-protein complexes of the two light-harvesting systems together with other intrinsic membrane proteins such as the cyt f / cyt b6 complex and the CF0 component of the coupling factor. Little or no attention, however, has been paid to the possible role of the membrane lipid fraction in thylakoid membrane organisation. This paper is directed at an examination of this problem.
Keywords
Thylakoid Membrane Intramembranous Particle Fatty Acid Substituent Fluid Mosaic Model Unheated ControlPreview
Unable to display preview. Download preview PDF.
References
- Andersson B and Anderson JM (1980) Biochim. Biophys. Acta 593, 427–440.PubMedCrossRefGoogle Scholar
- Armond PA, Björkman O, Staehelin LA (1980) Biochim. Biophys. Acta 601, 433–462.PubMedCrossRefGoogle Scholar
- Armond, PA, Schreiber, U, Björkman O (1978) Plant Physiol. 61, 411–415.PubMedCrossRefGoogle Scholar
- Arntzen CJ (1978) In “Current Topics in Bioenergetics Vol. 8”, (Sanadi DR, Vernon LP, eds.) pp. 111–160, Academic Press, New York.Google Scholar
- Berry J and Björkman O (1980) Ann. Rev. Plant Physiol. 31, 491–543.CrossRefGoogle Scholar
- Gounaris K, Sen A, Brain APR, Quinn PJ. Williams WP (1983a) Biochim. Biophys. Acta 728, 129–139.CrossRefGoogle Scholar
- Gounaris K, Brain APR, Quinn PJ, Williams WP (1983b) FEBS Lett. 153, 47–51.CrossRefGoogle Scholar
- Heinz E, Siefermann-Harms D (1981) FEBS Lett. 124, 105–111.CrossRefGoogle Scholar
- Murphy DJ (1982) FEBS Lett. 150, 19–26.CrossRefGoogle Scholar
- Pearcy RW, Berry JA, Fork DC (1977) Plant Physiol. 59, 873–878.PubMedCrossRefGoogle Scholar
- Quinn PJ, Williams WP (1983) Biochim. Biophys. Acta 737, 223–266.CrossRefGoogle Scholar
- Quinn PJ, Gounaris K, Sen A, Williams WP (1982) In “Biochemistry and Metabolism of Plant Lipids”, (Wintermans JFGM, Kuiper PJC, eds.) pp. 327–335, Elsevier, Amsterdam.Google Scholar
- Schreiber U, Armond PA (1978) Biochim. Biophys. Acta 502, 138–151.PubMedCrossRefGoogle Scholar
- Sen A, Williams WP, Brain APR, Dickens MJ, Quinn PJ (1981) Nature 293, 488–490.PubMedCrossRefGoogle Scholar
- Sen A, Brain APR, Quinn PJ, Williams WP (1982) Biochim. Biophys. Acta 686, 215–224.PubMedCrossRefGoogle Scholar
- Siefermann-Harms D, Ross JW, Kaneshiro KH, Yamamoto HY (1982) FEBS Lett. 159, 191–196.CrossRefGoogle Scholar
- Staehelin LA, Armond PA, Miller KR (1977) Brookhaven Symp. Biol. 28, 278–315.Google Scholar
- Stidham MA, Uribe EG, Williams GJ (1982) Plant Physiol. 69, 929–934.PubMedCrossRefGoogle Scholar
- Williams WP, Sen A, Quinn PJ (1982) Trans. Biochem. Soc. 10, 335–338.Google Scholar