Proteins in Different <i>Synechocystis</i> Compartments Have Distinguishing N-Terminal Features:  A Combined Proteomics and Multivariate Sequence Analysis

Rajalahti, Tarja; Huang, Fang; Klement, Maria Rosén; Pisareva, Tatiana; Edman, Maria C.; Sjöstróm, Michael; Wieslander, Åke; Norling, Birgitta

doi:10.1021/pr0605973

Cited by 29 publications

(35 citation statements)

References 101 publications

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“…A final point, PSB27 is present in cyanobacteria as well as land plants (16,32). In cyanobacteria PSB27 is tightly associated with the thylakoid membrane via an N-terminal lipid modification that is absent in PSB27 from land plants (33).…”

Section: Mutant Line Accumulates Less Anthocyanin and Produces More Rosmentioning

confidence: 99%

PSB27: A thylakoid protein enabling Arabidopsis to adapt to changing light intensity

Hou

Garcia

et al. 2015

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

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In earlier studies we have identified FKBP20-2 and CYP38 as soluble proteins of the chloroplast thylakoid lumen that are required for the formation of photosystem II supercomplexes (PSII SCs). Subsequent work has identified another potential candidate functional in SC formation (PSB27). We have followed up on this possibility and isolated mutants defective in the PSB27 gene. In addition to lack of PSII SCs, mutant plants were severely stunted when cultivated with light of variable intensity. The stunted growth was associated with lower PSII efficiency and defective starch accumulation. In response to high light exposure, the mutant plants also displayed enhanced ROS production, leading to decreased biosynthesis of anthocyanin. Unexpectedly, we detected a second defect in the mutant, namely in CP26, an antenna protein known to be required for the formation of PSII SCs that has been linked to state transitions. Lack of PSII SCs was found to be independent of PSB27, but was due to a mutation in the previously described cp26 gene that we found had no effect on light adaptation. The present results suggest that PSII SCs, despite being required for state transitions, are not associated with acclimation to changing light intensity. Our results are consistent with the conclusion that PSB27 plays an essential role in enabling plants to adapt to fluctuating light intensity through a mechanism distinct from photosystem II supercomplexes and state transitions.photosystem | PSII supercomplex | photosynthesis | anthocyanin biosynthesis | reactive oxygen species P hotosynthetic light reactions entail the coordinated function of several large membrane complexes: photosystem I (PSI), photosystem II (PSII), cytochrome b6f complex, and CF 0 -CF 1 complex. PSII catalyzes the initial step of photosynthesis, the light-dependent oxidation of water that yields molecular oxygen and reduced plastoquinone. The native form of PSII residing in the thylakoid membrane is believed to be organized into several types of supercomplexes (SCs), including the PSII core and the peripheral light harvesting complex II (LHCII), that play a primary role in the harvesting of light, transfer of excitation energy to the reaction center and regulation of light utilization. Several monomeric antenna proteins including CP24, CP26, and CP29 regulate the interaction of the PSII core with LHCII trimers (1-4). Regulation is achieved through photoprotective mechanisms that dissipate absorbed excess energy as heat in response to stress conditions such as high light intensity (5, 6).In natural settings, both the intensity and the spectral quality of light vary extensively, sometimes within very short periods. The changes in light intensity result in imbalanced excitation of PSI and PSII, and with that may lower the efficiency of the photosynthetic light reactions. In acclimating to the changing conditions, plants modify their thylakoid proteins and reorganize their photosynthetic machinery (7,8). In a rapid response, designated state transitions (9), LHCII associates...

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Section: Mutant Line Accumulates Less Anthocyanin and Produces More Rosmentioning

confidence: 99%

PSB27: A thylakoid protein enabling Arabidopsis to adapt to changing light intensity

Hou

Garcia

et al. 2015

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

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“…PCC 6803 (hereafter referred to as Synechocystis) genome, as well as all other completely sequenced cyanobacterial genomes, contains only a single set of genes encoding the subunits of the Sec and Tat translocons (17)(18)(19). This suggests that the same translocation machineries are working in plasma and thylakoid membranes and this in turn indicates that information additional to the signal sequence is needed for correct targeting (20,21). The question of where in the intricate Synechocystis membrane system translocation and protein sorting takes place is still subject for intense research.…”

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confidence: 99%

“…Although the overall sequence identity of leader peptidases from various species is relatively low, five conserved regions were identified in the catalytic domain, called boxes B, C, D, and E, as well as the membrane anchor domain A (22,23). Both LepB1 and LepB2 in Synechocystis have the conserved A-E boxes (21,23), including the invariant amino acid residues demonstrated to be essential for catalytic activity. No other proteins with these conserved regions are found in the Synechocystis genome.…”

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confidence: 99%

Deletion of Synechocystis sp. PCC 6803 Leader Peptidase LepB1 Affects Photosynthetic Complexes and Respiration

Zhang

Selão

Pisareva

et al. 2013

Molecular & Cellular Proteomics

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The cyanobacterium Synechocystis sp. PCC 6803 possesses two leader peptidases, LepB1 (Sll0716) and LepB2 (Slr1377), responsible for the processing of signal peptide-containing proteins. Deletion of the gene for LepB1 results in an inability to grow photoautotrophically and an extreme light sensitivity. Here we show, using a combination of Blue Native/SDS-PAGE, Western blotting and iTRAQ analysis, that lack of LepB1 strongly affects the cell's ability to accumulate wild-type levels of both photosystem I (PSI) and cytochrome (Cyt) b 6 f complexes. The impaired assembly of PSI and Cyt b 6 f is considered to be caused by the no or slow processing of the integral subunits PsaF and Cyt f respectively. In particular, PsaF, one of the PSI subunits, was found incorporated into PSI in its unprocessed form, which could influence the assembly and/or stability of PSI. In contrast to these results, we found the amount of assembled photosystem II (PSII) unchanged, despite a slower processing of PsbO. Thus, imbalance in the ratios of PSI and Cyt b 6 f to photosystem II leads to an imbalanced photosynthetic electron flow upand down-stream of the plastoquinone pool, resulting in the observed light sensitivity of the mutant. We conclude that LepB1 is the natural leader peptidase for PsaF, PsbO, and Cyt f. The maturation of PsbO and Cyt f can be partially performed by LepB2, whereas PsaF processing is completely dependent on LepB1. iTRAQ analysis also revealed a number of indirect effects accompanying the mutation, primarily a strong induction of the CydAB oxidase as well as a significant decrease in phycobiliproteins and chlorophyll/heme biosynthesis enzymes. Molecular

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“…The Psb27 protein is widely present in cyanobacteria as well as higher plants and is localized to the thylakoid lumen (23,24). Cyanobacterial Psb27 is tightly associated with the thylakoid membrane via its N-terminal lipoprotein motif, which is absent in higher plants (25).…”

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confidence: 99%

LPA19, a Psb27 Homolog in Arabidopsis thaliana, Facilitates D1 Protein Precursor Processing during PSII Biogenesis

Wei

Guo

Ouyang

et al. 2010

Journal of Biological Chemistry

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The biogenesis and assembly of photosystem II (PSII) are mainly regulated by the nuclear-encoded factors. To further identify the novel components involved in PSII biogenesis, we isolated and characterized a high chlorophyll fluorescence low psii accumulation19 (lpa19) mutant, which is defective in PSII biogenesis. LPA19 encodes a Psb27 homolog (At1g05385). Interestingly, another Psb27 homolog (At1g03600) in Arabidopsis was revealed to be required for the efficient repair of photodamaged PSII. These results suggest that the Psb27 homologs play distinct functions in PSII biogenesis and repair in Arabidopsis. Chloroplast protein labeling assays showed that the C-terminal processing of D1 in the lpa19 mutant was impaired. Protein overlay assays provided evidence that LPA19 interacts with D1, and coimmunoprecipitation analysis demonstrated that LPA19 interacts with mature D1 (mD1) and precursor D1 (pD1). Moreover, LPA19 protein was shown to specifically interact with the soluble C terminus present in the precursor and mature D1 through yeast two-hybrid analyses. Thus, these studies suggest that LPA19 is involved in facilitating the D1 precursor protein processing in Arabidopsis. Photosystem II (PSII),2 which catalyzes light-driven water oxidation and plastoquinone reduction, is a large pigment-protein complex found in the thylakoid membranes of cyanobacteria and chloroplasts. In higher plants, PSII contains more than 20 subunits including both integral and peripheral proteins (1, 2). The PSII reaction center proteins D1 and D2 bind most of the redox components essential for primary charge separation. Light energy transfer to the PSII reaction center is mediated by the intrinsic chlorophyll a-binding proteins, CP47 and CP43. The oxygen evolving complex, located on the luminal side of PSII, consists of a manganese cluster and several extrinsic proteins (3-6).

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Proteins in Different Synechocystis Compartments Have Distinguishing N-Terminal Features: A Combined Proteomics and Multivariate Sequence Analysis

Cited by 29 publications

References 101 publications

PSB27: A thylakoid protein enabling Arabidopsis to adapt to changing light intensity

PSB27: A thylakoid protein enabling Arabidopsis to adapt to changing light intensity

Deletion of Synechocystis sp. PCC 6803 Leader Peptidase LepB1 Affects Photosynthetic Complexes and Respiration

LPA19, a Psb27 Homolog in Arabidopsis thaliana, Facilitates D1 Protein Precursor Processing during PSII Biogenesis

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