Consequences of Light Induced D1-Protein Degradation on Thylakoid Membrane Organization

1990 ◽  
pp. 1383-1386
Author(s):  
I. Virgin ◽  
T. Hundal ◽  
S. Styring ◽  
B. Andersson
Keyword(s):  
Protein Degradation ◽  
Thylakoid Membrane ◽  
D1 Protein ◽  
Membrane Organization

Phosphorylation of PS II polypeptides inhibits D1 protein-degradation and increases PS II stability

1996 ◽  
Vol 50 (3) ◽  
pp. 257-269 ◽  
Author(s):  
Volker Ebbert ◽  
Doris Godde
Keyword(s):  
Protein Degradation ◽  
D1 Protein ◽  
Ps Ii

scholarly journals New Insights in Thylakoid Membrane Organization

2005 ◽  
Vol 46 (9) ◽  
pp. 1443-1451 ◽  
Author(s):  
Stephan Pfeiffer ◽  
Karin Krupinska
Keyword(s):  
Thylakoid Membrane ◽  
Membrane Organization

Degradation of unassembled and damaged thylakoid proteins

2001 ◽  
Vol 29 (4) ◽  
pp. 427-430 ◽  
Author(s):  
Z. Adam ◽  
O. Ostersetzer
Keyword(s):  
Thylakoid Membrane ◽  
D1 Protein ◽  
Thylakoid Membranes ◽  
Reaction Centre ◽  
Ps Ii ◽  
Plant Genomes ◽  
Thylakoid Membrane Proteins ◽  
Luminal Side ◽  
Cytochrome Complex ◽  
Aaa Protein

To study protein degradation in thylakoid membranes we identified, characterized and cloned thylakoid proteases, and then linked them to known proteolytic processes. Several families of chloroplast proteases were identified and characterized to different extents. FtsH, an ATP-dependent metalloprotease that belongs to the AAA-protein family, was found to be integral to the thylakoid membrane, facing the stroma. It is involved in both the degradation of unassembled subunits of membrane complexes, such as the Rieske Fe-S protein of the cytochrome complex, and the degradation of oxidatively damaged proteins such as the D1 protein of the photosystem II (PS II) reaction centre. Plant genomes contain multiple isomers of this protease but the functional significance of this multiplication is not clear yet. A second protease, the serine ATP-independent DegP, was found to be strongly associated with the luminal side of the thylakoid membrane. Although a specific role has not yet assigned for it, its location suggests that it can degrade luminal soluble proteins as well as luminally exposed regions of thylakoid membrane proteins.

A Thylakoid-Located Two-Pore K+ Channel Controls Photosynthetic Light Utilization in Plants

Science ◽  
2013 ◽  
Vol 342 (6154) ◽  
pp. 114-118 ◽  
Author(s):  
Luca Carraretto ◽  
Elide Formentin ◽  
Enrico Teardo ◽  
Vanessa Checchetto ◽  
Martino Tomizioli ◽  
...  
Keyword(s):  
Thylakoid Membrane ◽  
Proton Motive Force ◽  
Motive Force ◽  
K Channel ◽  
Channel Activity ◽  
Membrane Organization ◽  
Physiological Functions ◽  
Environmental Stimuli ◽  
Light Utilization ◽  
Selective Channel

The size of the light-induced proton motive force (pmf) across the thylakoid membrane of chloroplasts is regulated in response to environmental stimuli. Here, we describe a component of the thylakoid membrane, the two-pore potassium (K+) channel TPK3, which modulates the composition of the pmf through ion counterbalancing. Recombinant TPK3 exhibited potassium-selective channel activity sensitive to Ca2+ and H+. In Arabidopsis plants, the channel is found in the thylakoid stromal lamellae. Arabidopsis plants silenced for the TPK3 gene display reduced growth and altered thylakoid membrane organization. This phenotype reflects an impaired capacity to generate a normal pmf, which results in reduced CO2 assimilation and deficient nonphotochemical dissipation of excess absorbed light. Thus, the TPK3 channel manages the pmf necessary to convert photochemical energy into physiological functions.

Constructed deletions in lumen-exposed regions of the D1 protein in the cyanobacterium Synechocystis 6803: Effects on D1 insertion and accumulation in the thylakoid membrane, and on Photosystem II assembly

1996 ◽  
Vol 49 (2) ◽  
pp. 131-140 ◽  
Author(s):  
Gaza Salih ◽  
Ronney Wiklund ◽  
Taina Tyystj�rvi ◽  
Pirkko M�enp�� ◽  
Catherine Gerez ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Thylakoid Membrane ◽  
D1 Protein ◽  
Synechocystis 6803
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