Thylakoid membranes proteins

Cramer, W. A., et al., 1985. Topogi aphy and function of thylakoid membrane proteins. Trends in Biochemical Sciences 10 125-129. 

Dekker, J.P. and Boekema, E.J. 2005. Supramolecular organization of thylakoid membrane proteins in green plants. Biochim. Biophys. Acta 1706 12-39. 

The inner envelope membrane proteins have a cleavable N-terminal transit peptide, as well as some hydrophobic domain (s) in their mature portion. There are two possibilities on the role of this hydrophobic domain it may work as an N-terminal signal peptide after the translocation into the stroma and the subsequent cleavage of the transit peptide. Alternatively, it may work as a stop-transfer signal. One more important question is how the distinction is made between the outer membrane proteins, the inner membrane proteins, and the thylakoid membrane proteins. It is still an enigma. 

Zurawski, G., H.J, Bohnert, P.R. Whitfield, and W. Bottomley (1982). Nucleotide sequence of the gene for the Mr 32000 thylakoid membrane protein from Spinacia oleracea and Nicotiana debneyi predicts a totally conserved primary translation product of Mr 38,950. Proc. Natl. Acad. Sci., 79 7699-7703. 

Phosporylation of thylakoid membrane proteins which occurs in vivo in C. reinhardtii, cannot be accounted for by a single kinase activity. We consider the existence of two distinct kinases which differ in substrate specificity an activable LHC-kinase, the activity of which is controlled by the b6/f complex, and a continuously active PSII-kinase which is LHC-dependent. A model is proposed which involves an interaction between three groups of phosphoproteins. This interaction could arise either from a phosphotransferase process or from a sequence of substrate-induced modifications. 

Gavel, Y, Steppuhn,J., Herrmann, R., and von Heijne, G. (1991). The positive-inside rule applies to thylakoid membrane proteins. FEBS Lett. 282, 41-46. 

Figure 5 Western Blot Analysis of Chi Antenna Proteins Thylakoid membrane proteins were isolated from control and Chi b-less C. reinhardtii. Arrows mark the position of the major constituents of the LHC-II.

Fig. 5. Cytochrome t. (A) Its location in the thylakoid membrane (B) Amino-acid sequences for turnip Cyt f(Brassica campestris, B.C.), spinach Spinacia oleracea, S.o.) and Nostoc PCC 7906 (7906) (C) Hydropathy plot and (D) Topological model. (B) from Gray (1992) Cytochrome f Structure, function and biosynthesis. Photosynthesis Res 34 361 (C) from Widger, Cramer, Herrmann and Trebst (1985) Topography and function of thylakoid membrane proteins. Trends Biochem Sci 10 126.

Dalbey, R. E., and A. Kuhn. 2000. Evolutionarily related insertion pathways of bacterial, mitochondrial, and thylakoid membrane proteins. Ann. Rev. Cell Devel. Biol. 16 51-87. 

Tae GS, Black MT, Cramer WA et al. Thylakoid membrane protein topography transmembrane orientation of the chloroplast cytochrome b559 psbE gene product. Biochemistry 1988 27 9075-9080. 

Fig.2. Electropherogram (A) and autoradiograph (B) of thylakoid membrane proteins. For the methionine-labeled samples, intact...

Table 1 Relative abundances of LHC apoproteins in rice and barley mutants determined on the basis of thylakoid membrane proteins.

The biogenesis of thylakoid proteins is a complex issue since these proteins are synthesised by two distinct genetic systems. Of particular complexity and interest is the biogenesis of cytoplasmically-synthesised thylakoid lumen proteins, since these proteins must cross three membranes to reach their sites of function. Previous work on one such protein, plastocyanin, indicated that the import of this protein can be divided into two phases. Plastocyanin is initially synthesised as a precursor, which is post-translationally imported across the double-membrane envelope and processed to an intermediate form by a stromal processing peptidase, SPP. The intermediate is then transferred across the thylakoid membrane and processed by a second thylakoidal processing peptidase, TPP (1-3). TPP is an integral thylakoid membrane protein with the active site on the lumenal face of the membrane the enzyme is located exclusively in non-appressed, "stromal" lamellae (4.5). 

Fig. 3 A) Thylakoid membrane proteins and soluble proteins from gametes, 60 hours old. The M protein is not found in the thylakoid membrane fraction but is retained in the 150 000 g supernatant (45 min. centrifugation). B) Ma is immunodetected by a-cytf among the soluble proteins from the gametes.

Fig. 3 Detection of BLIP after different periods of illumination. Pea seedlings were grown in total darkness for six days and then illuminated as indicated. Thylakoid membrane proteins were isolated, resolved on a 12.5 % SDS-gel and transferred to a nitrocellulose sheet by a semy dry blotting system. BLIP was immunodetected with an BLIP specific primary antibody and a horse radish peroxidase conjugated secondary antibody.

Jasmonic acid treatment has been reported to result in the inhibition of Hill reaction activity and flash-Oj evolution [73], alteration of intra-chloroplast structure [74] and chlorophyll fluorescence parameters [75], a change in the polypeptide pattern of thylakoid membrane proteins [76] and ultimately a decreased photosynthetic rate [77]. An increase in the rate of dark respiration, photorespiration and stomatal resistance to COj diffusion has also been observed [77,78]. 

A notion that the proton-buffering domains sequestered in thylakoid membranes may be involved in proton diffusion has been elaborated on in several laboratories [59, 113, 125-130]. There is much data indicating the existence of membrane-bound proton pools which are not in rapidly established equilibrium with protons in the bulk phases (see, for references, [113]). These membrane-buried slow exchanging proton-accepting groups belong to the thylakoid membrane proteins. Under normal conditions, the intramem-... 

Peters, J. S. Chin, C. K. (2003). Inhibition of photosynthetic electron transport by palmitoleic acid is partially correlated to loss of thylakoid membrane proteins. Plant Physiol Biochem., 41, 117-124. 

Carotenoids, lutein and xanthophylls are also bound to thylakoid membrane proteins but the binding mechanism is less well anderstood. In the case of B-carotene, it is believed that it is orientated with its long axis parallel to the membrane normal in PSI and PSII. This implies a different binding mechanism to the chlorophylls. 

Kyle, D.J. and Amtzen, C.J., Thylakoid membrane protein phosphorylation selectively alters the local membrane surface charge near the primary acceptor of Photosystem II, Photochem. Photo-biophys., 5,11, 1983. 

Schmidt 0 (1983) Spatial arrangement of thylakoid membrane proteins analysed by controlled proteolytic digestion, Photosynthetica 17, 69-76. Sofrova D Sacka H Masojidek J and Leblova S (1980) Functional and structural changes of cyanobacterial thylakoids after treatment with pronase and lipase, Photosynthetica 14, 198-203. 

Kyle D J, Haworth P and Arntzen C J (1982) Thylakoid membrane protein phosphorylation leads to a decrease in connectivity between photosystem II reaction centers, Biochim. Biophys. Acta 680, 336-342. 

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