Close vicinity of Lhc b1 and Lhc b4 in Photosystem II

Miao, Jihong; Irrgang, Klaus−Dieter; Salnikow, Johann; Franke, P.; Vater, Joachim

doi:10.1046/j.1432-1327.1998.2570586.x

Cited by 4 publications

(2 citation statements)

References 51 publications

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“…While this approach is classically and commonly used to study supramolecular structures, there are only a few success stories in plant biology. Since 1998 and the article of Miao and co-workers (Miao et al, 1998) on PSII very few works based on MS as final techniques have been published (Rohila et al, 2004;Sommer et al, 2006;Ahrman et al, 2007;Gertz et al, 2007;Tetlow et al, 2008). So far, the most attractive study used dithiobis (succinimidylpropionate)-a reversible protein cross-linking agent-to show that the plant-specific thylakoid-soluble phosphoprotein of 9 kDa (TSP9) is part of the PSII-LHCII supercomplex and that this soluble mobile phosphoprotein is in close association with LHCII as well as the periphery of the PS, suggesting involvement in regulation of photosynthetic light harvesting (Hansson et al, 2007).…”

Section: Dynamic Protein Interactionsmentioning

confidence: 99%

Plant organelle proteomics: Collaborating for optimal cell function

Agrawal¹,

Bourguignon

Rolland

et al. 2010

Mass Spectrometry Reviews

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Organelle proteomics describes the study of proteins present in organelle at a particular instance during the whole period of their life cycle in a cell. Organelles are specialized membrane bound structures within a cell that function by interacting with cytosolic and luminal soluble proteins making the protein composition of each organelle dynamic. Depending on organism, the total number of organelles within a cell varies, indicating their evolution with respect to protein number and function. For example, one of the striking differences between plant and animal cells is the plastids in plants. Organelles have their own proteins, and few organelles like mitochondria and chloroplast have their own genome to synthesize proteins for specific function and also require nuclear-encoded proteins. Enormous work has been performed on animal organelle proteomics. However, plant organelle proteomics has seen limited work mainly due to: (i) inter-plant and inter-tissue complexity, (ii) difficulties in isolation of subcellular compartments, and (iii) their enrichment and purity. Despite these concerns, the field of organelle proteomics is growing in plants, such as Arabidopsis, rice and maize. The available data are beginning to help better understand organelles and their distinct and/or overlapping functions in different plant tissues, organs or cell types, and more importantly, how protein components of organelles behave during development and with surrounding environments. Studies on organelles have provided a few good reviews, but none of them are comprehensive. Here, we present a comprehensive review on plant organelle proteomics starting from the significance of organelle in cells, to organelle isolation, to protein identification and to biology and beyond. To put together such a systematic, in-depth review and to translate acquired knowledge in a proper and adequate form, we join minds to provide discussion and viewpoints on the collaborative nature of organelles in cell, their proper function and evolution.

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Section: Dynamic Protein Interactionsmentioning

confidence: 99%

Plant organelle proteomics: Collaborating for optimal cell function

Agrawal¹,

Bourguignon

Rolland

et al. 2010

Mass Spectrometry Reviews

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“…The transmembrane folding pattern of CP29 is also expected to be similar to that of LHC II with three membrane-spanning ␣-helices and a fourth amphipathic helix. Chemical cross-linking, sequence analysis, mass spectrometry and immunolabeling experiments established that CP29 is adjacent to Lhcb1 (15,16). The pigmentprotein complex from maize thylakoids can be phosphorylated under cold-stress conditions (17) and the post-translationally modified form reveals different spectroscopic properties (18).…”

Section: Introductionmentioning

confidence: 98%

Assignment of the Lowest QY-state and Spectral Dynamics of the CP29 Chlorophyll a/b Antenna Complex of Green Plants: A Hole-burning Study ‡

Pieper

Irrgang

Rätsep

et al. 2007

Photochemistry and Photobiology

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Low‐temperature absorption, fluorescence and persistent nonphotochemical hole‐burned spectra are reported for the CP29 chlorophyll (Chl) a/b antenna complex of photosystem II of green plants. The absorption‐origin band of the lowest Qy‐state lies at 678.2 nm and carries a width of ∼130 cm−1 that is dominated by inhomogeneous broadening at low temperatures. Its absorption intensity is equivalent to that of one of the six Chl a molecules of CP29. The absence of a significant satellite hole structure produced by hole burning, within the absorption band of the lowest state, indicates that the associated Chl a molecule is weakly coupled to the other Chl and, therefore, that the lowest‐energy state is highly localized on a single Chl a molecule. The electron–phonon coupling of the 678.2 nm state is weak with a Huang–Rhys factor S of 0.5 and a peak phonon frequency (ωm) of ∼20 cm−1. These values give a Stokes shift (2Sωm) in good agreement with the measured positions of the absorption band at 678.2 nm and a fluorescence‐origin band at 679.1 nm. Zero‐phonon holes associated with the lowest state have a width of ∼0.05 cm−1 at 4.2 K, corresponding to a total effective dephasing time of ∼400 ps. The temperature dependence of the zero‐phonon holewidth indicates that this time constant is dominated at temperatures below 8 K by pure dephasing/spectral diffusion due to coupling of the optical transition to the glass‐like two‐level systems of the protein. Zero‐phonon holewidths obtained for the Chl b bands at 638.5 and 650.0 nm, at 4.2 K, lead to lower limits of 900 ± 150 fs and 4.2 ± 0.3 ps, respectively, for the Chl b→ Chl a energy‐transfer times. Downward energy transfer from the Chl a state(s) at 665.0 nm occurs in 5.3 ± 0.6 ps at 4.2 K.

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Distal and Extrinsic Photosystem II Antennas

Green

Gantt

2005

Advances in Photosynthesis and Respiration

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Close vicinity of Lhc b1 and Lhc b4 in Photosystem II

Cited by 4 publications

References 51 publications

Plant organelle proteomics: Collaborating for optimal cell function

Plant organelle proteomics: Collaborating for optimal cell function

Assignment of the Lowest QY-state and Spectral Dynamics of the CP29 Chlorophyll a/b Antenna Complex of Green Plants: A Hole-burning Study ‡

Distal and Extrinsic Photosystem II Antennas

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