scholarly journals TLP18.3, a novel thylakoid lumen protein regulating photosystem II repair cycle

2007 ◽  
Vol 406 (3) ◽  
pp. 415-425 ◽  
Author(s):  
Sari Sirpiö ◽  
Yagut Allahverdiyeva ◽  
Marjaana Suorsa ◽  
Virpi Paakkarinen ◽  
Julia Vainonen ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Protein Complexes ◽  
D1 Protein ◽  
Proteome Analysis ◽  
Growth Conditions ◽  
Dual Function ◽  
High Turnover ◽  
Thylakoid Lumen ◽  
Chain Complexes ◽  
Nascent Chain

A proteome analysis of Arabidopsis thaliana thylakoid-associated polysome nascent chain complexes was performed to find novel proteins involved in the biogenesis, maintenance and turnover of thylakoid protein complexes, in particular the PSII (photosystem II) complex, which exhibits a high turnover rate. Four unknown proteins were identified, of which TLP18.3 (thylakoid lumen protein of 18.3 kDa) was selected for further analysis. The Arabidopsis mutants (SALK_109618 and GABI-Kat 459D12) lacking the TLP18.3 protein showed higher susceptibility of PSII to photoinhibition. The increased susceptibility of ΔTLP18.3 plants to high light probably originates from an inefficient reassembly of PSII monomers into dimers in the grana stacks, as well as from an impaired turnover of the D1 protein in stroma exposed thylakoids. Such dual function of the TLP18.3 protein is in accordance with its even distribution between the grana and stroma thylakoids. Notably, the lack of the TLP18.3 protein does not lead to a severe collapse of the PSII complexes, suggesting a redundancy of proteins assisting these particular repair steps to assure functional PSII. The ΔTLP18.3 plants showed no clear visual phenotype under standard growth conditions, but when challenged by fluctuating light during growth, the retarded growth of ΔTLP18.3 plants was evident.

Evidence for a dual function of the herbicide-binding D1 protein in photosystem II

FEBS Letters ◽  
1986 ◽  
Vol 205 (2) ◽  
pp. 269-274 ◽  
Author(s):  
James G. Metz ◽  
Himadri B. Pakrasi ◽  
Michael Seibert ◽  
Charles J. Arntzer
Keyword(s):  
Photosystem Ii ◽  
D1 Protein ◽  
Dual Function ◽  
Herbicide Binding

scholarly journals Synthesis and assembly of thylakoid protein complexes: multiple assembly steps of photosystem II

2005 ◽  
Vol 388 (1) ◽  
pp. 159-168 ◽  
Author(s):  
Anne ROKKA ◽  
Marjaana SUORSA ◽  
Ammar SALEEM ◽  
Natalia BATTCHIKOVA ◽  
Eva-Mari ARO
Keyword(s):  
Photosystem Ii ◽  
Molecular Mass ◽  
Spinacia Oleracea ◽  
Protein Complexes ◽  
D1 Protein ◽  
Oxygen Evolving Complex ◽  
Reaction Centre ◽  
Light Intensities ◽  
Thylakoid Protein

To study the synthesis and assembly of multisubunit thylakoid protein complexes, we performed [35S]Met pulse and chase experiments with isolated chloroplasts and intact leaves of spinach (Spinacia oleracea L.), followed by Blue Native gel separation of the (sub)complexes and subsequent identification of the newly synthesized and assembled protein subunits. PSII (photosystem II) core subunits were the most intensively synthesized proteins, particularly in vitro and at high light intensities in vivo, and could be sequestered in several distinct PSII subassemblies. Newly synthesized D1 was first found in the reaction centre complex that also contained labelled D2 and two labelled low-molecular-mass proteins. The next biggest PSII subassembly contained CP47 also. Then PsbH was assembled together with at least two other labelled chloroplast-encoded low-molecular-mass subunits, PsbM and PsbTc, and a nuclear-encoded PsbR. Subsequently, CP43 was inserted into the PSII complex concomitantly with PsbK. These assembly steps seemed to be essential for the dimerization of PSII core monomers. Intact PSII core monomer was the smallest subcomplex harbouring the newly synthesized 33 kDa oxygen-evolving complex protein PsbO. Nuclear-encoded PsbW was synthesized only at low light intensities concomitantly with Lhcb polypeptides and was distinctively present in PSII–LHCII (where LHC stands for light-harvesting complex) supercomplexes. The PsbH protein, on the contrary, was vigorously synthesized and incorporated into PSII core monomers together with the D1 protein, suggesting an intrinsic role for PsbH in the photoinhibition-repair cycle of PSII.

scholarly journals Transcriptome and proteome analysis suggest enhanced photosynthesis in tetraploid Liriodendron sino-americanum

2021 ◽  
Author(s):  
Tingting Chen ◽  
Yu Sheng ◽  
Zhaodong Hao ◽  
Xiaofei Long ◽  
Fangfang Fu ◽  
...  
Keyword(s):  
Molecular Mechanisms ◽  
Protein Complexes ◽  
Proteome Analysis ◽  
Tree Height ◽  
Photosynthetic Electron Transport ◽  
Industrial Applications ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein ◽  
Photosynthesis Genes ◽  
Underlying Mechanisms

Abstract Polyploidy generally provides an advantage in phenotypic variation and growth vigor. However, the underlying mechanisms remain poorly understood. The tetraploid L. sino-americanum exhibits altered morphology compared to its diploid counterpart, including larger, thicker and deeper green leaves, bigger stomata, thicker stems and increased tree height. Such characteristics can be useful in ornamental and industrial applications. To elucidate the molecular mechanisms behind this variation, we performed a comparative transcriptome and proteome analysis. Our transcriptome data indicated that some photosynthesis genes and pathways were differentially altered and enriched in tetraploid L. sino-americanum, mainly related to F-type ATPase, the cytochrome b6/f complex, photosynthetic electron transport, the light harvesting chlorophyll protein complexes, photosystem I and II. Most of the differentially expressed proteins we could identify are also involved in photosynthesis. Our physiological results showed that tetraploids have an enhanced photosynthetic capacity, concomitant with great levels of sugar and starch in leaves. This suggests that tetraploid L. sino-americanum might experience comprehensive transcriptome reprogramming of genes related to photosynthesis. This study has especially emphasized molecular changes involved in photosynthesis that accompany polyploidy, and provides a possible explanation for the altered phenotype of polyploidy plants in comparison to their diploid form.

Breakdown of the photosystem II reaction center D1 protein under photoinhibitory conditions: identification and localization of the C-terminal degradation products

Biochemistry ◽  
1991 ◽  
Vol 30 (42) ◽  
pp. 10220-10226 ◽  
Author(s):  
Roberto Barbato ◽  
Giulia Friso ◽  
Maria Teresa Giardi ◽  
Fernanda Rigoni ◽  
Giorgio Mario Giacometti
Keyword(s):  
Photosystem Ii ◽  
Reaction Center ◽  
Degradation Products ◽  
D1 Protein

The Thylakoid FtsH Protease Plays a Role in the Light-Induced Turnover of the Photosystem II D1 Protein

2000 ◽  
Vol 12 (3) ◽  
pp. 419 ◽  
Author(s):  
Marika Lindahl ◽  
Cornelia Spetea ◽  
Torill Hundal ◽  
Amos B. Oppenheim ◽  
Zach Adam ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
D1 Protein ◽  
Ftsh Protease
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