Function of Chlorophylls and Carotenoids in Thylakoid Membranes: Chlorophylls Betweeen Pigment-Protein Complexes Might Function by Stabilizing the Membrane Structure

Author(s):  
Grimme ◽  
L. Horst ◽  
Jeanette S. Brown
2012 ◽  
Vol 169 (1) ◽  
pp. 65-71 ◽  
Author(s):  
Ewa Janik ◽  
Waldemar Maksymiec ◽  
Wojciech Grudziński ◽  
Wiesław I. Gruszecki

2012 ◽  
Vol 161 (1) ◽  
pp. 497-507 ◽  
Author(s):  
Helmut Kirchhoff ◽  
Richard M. Sharpe ◽  
Miroslava Herbstova ◽  
Robert Yarbrough ◽  
Gerald E. Edwards

1986 ◽  
Vol 41 (3) ◽  
pp. 284-290 ◽  
Author(s):  
Robert Carpentier ◽  
Roger M. Leblanc ◽  
Guy Bellemare

Pigment photobleaching was performed in thylakoid membranes of Hordeum vulgare (wild type, mutant Chlorina f2, Norfluranzon treated seedlings) and in pigment-protein complexes (CP-I and LHCP) isolated from H. vulgare and Chlamydomonas reinhardtii. Multiphasic kinetics were obtained in all of the above cases. Energy transfer towards pigments absorbing at longer wavelength is postulated as a general protection mechanism against photobleaching. This mechanism explains a substantial bleaching of carotenoids and a faster bleaching of chlorophyll aggregates, absorbing at long wavelength. These conclusions were valid for isolated complexes as well as for thylakoid membranes, although membranes were less sensitive to light.


2016 ◽  
Vol 97 (6) ◽  
pp. 1241-1249 ◽  
Author(s):  
Wang Yi-Bin ◽  
Liu Fang-Ming ◽  
Zhang Xiu-Fang ◽  
Zhang Ai-Jun ◽  
Wang Bin ◽  
...  

Ice algae have successfully adapted to the extreme environmental conditions in the Antarctic, however the underlying mechanisms involved in the regulation and response of thylakoid membranes and chloroplast to low-temperature stress are still not well understood. In this study, changes in pigment concentrations, lipids, fatty acids and pigment protein complexes in thylakoid membranes and chloroplast after exposure to low temperature conditions were investigated using the Antarctic ice algae Chlamydomonas sp. ICE-L. Results showed that the chloroplasts of Chlamydomonas sp. ICE-L are distributed throughout the cell except in the nuclear region in the form of thylakoid lamellas which exists in the gap between organelles and the starch granules. Also, the structure of mitochondria has no obvious change after cold stress. Concentrations of Chl a, Chl b, monogalactosyl diacylglycerol, digalactosyl diacylglycerol and fatty acids were also observed to exhibit changes with temperature, suggesting possible adaptations to cold environments. The light harvesting complex, lutein and β-carotene played an important role for adaptation of ICE-L, and increasing of monogalactosyl diacylglycerol and digalactosyl diacylglycerol improved the overall degree of unsaturation of thylakoid membranes, thereby maintaining liquidity of thylakoid membranes. The pigments, lipids, fatty acids and pigment-protein complexes maintained the stability of the thylakoid membranes and the normal physiological function of Chlamydomonas sp. ICE-L.


2010 ◽  
pp. 202-205
Author(s):  
N. Yu. Taran ◽  
◽  
I. P. Ozheredova ◽  
V. O. Storozhenko ◽  
N. B. Svetlova ◽  
...  

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 374 ◽  
Author(s):  
Aparna Nagarajan ◽  
Mowei Zhou ◽  
Amelia Y. Nguyen ◽  
Michelle Liberton ◽  
Komal Kedia ◽  
...  

Phycobilisomes (PBSs) are large (3–5 megadalton) pigment-protein complexes in cyanobacteria that associate with thylakoid membranes and harvest light primarily for photosystem II. PBSs consist of highly ordered assemblies of pigmented phycobiliproteins (PBPs) and linker proteins that can account for up to half of the soluble protein in cells. Cyanobacteria adjust to changing environmental conditions by modulating PBS size and number. In response to nutrient depletion such as nitrogen (N) deprivation, PBSs are degraded in an extensive, tightly controlled, and reversible process. In Synechococcus elongatus UTEX 2973, a fast-growing cyanobacterium with a doubling time of two hours, the process of PBS degradation is very rapid, with 80% of PBSs per cell degraded in six hours under optimal light and CO2 conditions. Proteomic analysis during PBS degradation and re-synthesis revealed multiple proteoforms of PBPs with partially degraded phycocyanobilin (PCB) pigments. NblA, a small proteolysis adaptor essential for PBS degradation, was characterized and validated with targeted mass spectrometry. NblA levels rose from essentially 0 to 25,000 copies per cell within 30 min of N depletion, and correlated with the rate of decrease in phycocyanin (PC). Implications of this correlation on the overall mechanism of PBS degradation during N deprivation are discussed.


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