scholarly journals Differential Mobility of Pigment-Protein Complexes in Granal and Agranal Thylakoid Membranes of C3 and C4 Plants

2012 ◽  
Vol 161 (1) ◽  
pp. 497-507 ◽  
Author(s):  
Helmut Kirchhoff ◽  
Richard M. Sharpe ◽  
Miroslava Herbstova ◽  
Robert Yarbrough ◽  
Gerald E. Edwards
Keyword(s):  
Protein Complexes ◽  
Thylakoid Membranes ◽  
C4 Plants ◽  
C3 And C4 Plants ◽  
Differential Mobility ◽  
Pigment Protein Complexes

Strong light-induced reorganization of pigment–protein complexes of thylakoid membranes in rye (spectroscopic study)

2012 ◽  
Vol 169 (1) ◽  
pp. 65-71 ◽  
Author(s):  
Ewa Janik ◽  
Waldemar Maksymiec ◽  
Wojciech Grudziński ◽  
Wiesław I. Gruszecki
Keyword(s):  
Spectroscopic Study ◽  
Protein Complexes ◽  
Thylakoid Membranes ◽  
Strong Light ◽  
Pigment Protein Complexes

Chlorophyll Photobleaching in Pigment-Protein Complexes

1986 ◽  
Vol 41 (3) ◽  
pp. 284-290 ◽  
Author(s):  
Robert Carpentier ◽  
Roger M. Leblanc ◽  
Guy Bellemare
Keyword(s):  
Energy Transfer ◽  
Hordeum Vulgare ◽  
Chlamydomonas Reinhardtii ◽  
Protein Complexes ◽  
Thylakoid Membranes ◽  
Wild Type ◽  
Protection Mechanism ◽  
Long Wavelength ◽  
Pigment Protein Complexes ◽  
Type Mutant

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.

Composition and regulation of thylakoid membrane of Antarctic ice microalgae Chlamydomonas sp. ICE-L in response to low-temperature environment stress

2016 ◽  
Vol 97 (6) ◽  
pp. 1241-1249 ◽  
Author(s):  
Wang Yi-Bin ◽  
Liu Fang-Ming ◽  
Zhang Xiu-Fang ◽  
Zhang Ai-Jun ◽  
Wang Bin ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Low Temperature ◽  
Protein Complexes ◽  
Thylakoid Membranes ◽  
Ice Algae ◽  
Stress Concentrations ◽  
Light Harvesting Complex ◽  
Pigment Protein Complexes ◽  
Environment Stress ◽  
The Antarctic

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.

scholarly journals Pigment-protein complexes of thylakoid membranes of Deschampsia antarctica Desv. plants

2010 ◽  
pp. 202-205
Author(s):  
N. Yu. Taran ◽  
◽  
I. P. Ozheredova ◽  
V. O. Storozhenko ◽  
N. B. Svetlova ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Thylakoid Membranes ◽  
Deschampsia Antarctica ◽  
Pigment Protein Complexes

scholarly journals Proteomic Insights into Phycobilisome Degradation, A Selective and Tightly Controlled Process in The Fast-Growing Cyanobacterium Synechococcus elongatus UTEX 2973

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 374 ◽  
Author(s):  
Aparna Nagarajan ◽  
Mowei Zhou ◽  
Amelia Y. Nguyen ◽  
Michelle Liberton ◽  
Komal Kedia ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Photosystem Ii ◽  
Doubling Time ◽  
Protein Complexes ◽  
Thylakoid Membranes ◽  
Synechococcus Elongatus ◽  
Nutrient Depletion ◽  
Reversible Process ◽  
Fast Growing ◽  
Pigment Protein Complexes

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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