The Membrane-Associated CpcG2-Phycobilisome in <i>Synechocystis</i>: A New Photosystem I Antenna

Kondo, Kazunori; Ochiai, Yuriko; Katayama, Mikio; Ikeuchi, Masahiko

doi:10.1104/pp.107.099267

Cited by 120 publications

(109 citation statements)

References 75 publications

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“…This may require stronger tightness of membrane association to perform such a different function. In support of this notion CpcG2 but not CpcG1 was found to contain a hydrophobic C-terminal segment that directly interacts with the thylakoid membrane or PSI (51). The two phycocyanobilin lyases CpcE and CpcF, which may function as a heterodimer and both are necessary for the chromophorylation of phycocyanin alphasubunit (52,53), also reside in the different clusters on the plot, suggesting that the two proteins may localize differently yet operate synergistically for the chromophorylation.…”

Section: (1)mentioning

confidence: 84%

Systematically Ranking the Tightness of Membrane Association for Peripheral Membrane Proteins (PMPs) *

Gao

Huang

et al. 2015

Molecular & Cellular Proteomics

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Large-scale quantitative evaluation of the tightness of membrane association for nontransmembrane proteins is important for identifying true peripheral membrane proteins with functional significance. Herein, we simultaneously ranked more than 1000 proteins of the photosynthetic model organism Synechocystis sp. PCC 6803 for their relative tightness of membrane association using a proteomic approach. Using multiple precisely ranked and experimentally verified peripheral subunits of photosynthetic protein complexes as the landmarks, we found that proteins involved in two-component signal transduction systems and transporters are overall tightly associated with the membranes, whereas the associations of ribosomal proteins are much weaker. Moreover, we found that hypothetical proteins containing the same domains generally have similar tightness. This work provided a global view of the structural organization of the membrane proteome with respect to divergent functions, and built the foundation for future investigation of the dynamic membrane proteome reorganization in response to different environmental or internal stimuli. Molecular & Cellular Proteomics

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Section: (1)mentioning

confidence: 84%

Systematically Ranking the Tightness of Membrane Association for Peripheral Membrane Proteins (PMPs) *

Gao

Huang

et al. 2015

Molecular & Cellular Proteomics

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“…This finding suggests that GL-induced CpcG2 posttranslationally stabilized PC, leading to PC accumulation, although this effect was not so dramatic in this study. Interestingly, CpcG2 possesses a hydrophobic helix at its C terminus and is implicated in energy distribution from PBS to photosystem I in S. 6803 (35)(36)(37). This finding may suggest that N. punctiforme increases not only the PE/PC ratio but also energy transfer to photosystem I under GL.…”

Section: Discussionmentioning

confidence: 97%

Cyanobacteriochrome CcaS regulates phycoerythrin accumulation in Nostoc punctiforme , a group II chromatic adapter

Hirose¹,

Narikawa

Katayama

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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126

137

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Responding to green and red light, certain cyanobacteria change the composition of their light-harvesting pigments, phycoerythrin (PE) and phycocyanin (PC). Although this phenomenon—complementary chromatic adaptation—is well known, the green light–sensing mechanism for PE accumulation is unclear. The filamentous cyanobacterium Nostoc punctiforme ATCC 29133 ( N. punctiforme ) regulates PE synthesis in response to green and red light (group II chromatic adaptation). We disrupted the green/red-perceiving histidine-kinase gene ( ccaS ) or the cognate response regulator gene ( ccaR ), which are clustered with several PE and PC genes ( cpeC - cpcG2-cpeR1 operon) in N. punctiforme . Under green light, wild-type cells accumulated a significant amount of PE upon induction of cpeC - cpcG2 - cpeR1 expression, whereas they accumulated little PE with suppression of cpeC - cpcG2 - cpeR1 expression under red light. Under both green and red light, the ccaS mutant constitutively accumulated some PE with constitutively low cpeC - cpcG2 - cpeR1 expression, whereas the ccaR mutant accumulated little PE with suppression of cpeC - cpcG2 - cpeR1 expression. The results of an electrophoretic mobility shift assay suggest that CcaR binds to the promoter region of cpeC - cpcG2 - cpeR1 , which contains a conserved direct-repeat motif. Taken together, the results suggest that CcaS phosphorylates CcaR under green light and that phosphorylated CcaR then induces cpeC - cpcG2 - cpeR1 expression, leading to PE accumulation. In contrast, CcaS probably represses cpeC - cpcG2 - cpeR1 expression by dephosphorylation of CcaR under red light. We also found that the cpeB-cpeA operon is partially regulated by green and red light, suggesting that the green light-induced regulatory protein CpeR1 activates cpeB-cpeA expression together with constitutively induced CpeR2.

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“…Two types of PBS with different linker proteins (CpcG1 and CpcG2) were found in the unicellular cyanobacterium Synechocystis sp. PCC 6803 (Kondo et al, 2007). One was a normal PBS consisting of a PC rod and APC core (CpcG1-PBS); the other was an abnormal PBS lacking APC (CpcG2-PBS) that seemed to transfer excitation energy preferentially to PSI (Kondo et al, 2007).…”

Section: Discussion Different Dynamic Changes Of Pbs Subunits and Psimentioning

confidence: 99%

“…PCC 6803 (Kondo et al, 2007). One was a normal PBS consisting of a PC rod and APC core (CpcG1-PBS); the other was an abnormal PBS lacking APC (CpcG2-PBS) that seemed to transfer excitation energy preferentially to PSI (Kondo et al, 2007). The b Average values from Supplemental Figure S8.…”

Section: Discussion Different Dynamic Changes Of Pbs Subunits and Psimentioning

confidence: 99%

Transformation of Thylakoid Membranes during Differentiation from Vegetative Cell into Heterocyst Visualized by Microscopic Spectral Imaging

2012

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Some filamentous cyanobacteria carry out oxygenic photosynthesis in vegetative cells and nitrogen fixation in specialized cells known as heterocysts. Thylakoid membranes in vegetative cells contain photosystem I (PSI) and PSII, while those in heterocysts contain predominantly PSI. Therefore, the thylakoid membranes change drastically when differentiating from a vegetative cell into a heterocyst. The dynamics of these changes have not been sufficiently characterized in situ. Here, we used time-lapse fluorescence microspectroscopy to analyze cells of Anabaena variabilis under nitrogen deprivation at approximately 295 K. PSII degraded simultaneously with allophycocyanin, which forms the core of the light-harvesting phycobilisome. The other phycobilisome subunits that absorbed shorter wavelengths persisted for a few tens of hours in the heterocysts. The wholethylakoid average concentration of PSI was similar in heterocysts and nearby vegetative cells. PSI was best quantified by selective excitation at a physiological temperature (approximately 295 K) under 785-nm continuous-wave laser irradiation, and detection of higher energy shifted fluorescence around 730 nm. Polar distribution of thylakoid membranes in the heterocyst was confirmed by PSI-rich fluorescence imaging. The findings and methodology used in this work increased our understanding of how photosynthetic molecular machinery is transformed to adapt to different nutrient environments and provided details of the energetic requirements for diazotrophic growth.

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The Membrane-Associated CpcG2-Phycobilisome in Synechocystis: A New Photosystem I Antenna

Cited by 120 publications

References 75 publications

Systematically Ranking the Tightness of Membrane Association for Peripheral Membrane Proteins (PMPs) *

Systematically Ranking the Tightness of Membrane Association for Peripheral Membrane Proteins (PMPs) *

Cyanobacteriochrome CcaS regulates phycoerythrin accumulation in Nostoc punctiforme , a group II chromatic adapter

Transformation of Thylakoid Membranes during Differentiation from Vegetative Cell into Heterocyst Visualized by Microscopic Spectral Imaging

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