The <i>Synechocystis</i> sp PCC 6803 Oxa1 Homolog Is Essential for Membrane Integration of Reaction Center Precursor Protein pD1

Ossenbühl, Friedrich; Inaba-Sulpice, Masami; Meurer, Jörg; Soll, Jürgen; Eichacker, Lutz A.

doi:10.1105/tpc.106.043646

Cited by 52 publications

(33 citation statements)

References 40 publications

(39 reference statements)

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“…The early PSII assembly factors Slr1471 and YCF48 accumulated predominantly in TMs, but substantial amounts of these proteins, especially YCF48, were also detected in PDM fractions, underlining a role of PDMs during early PSII assembly ( Fig. 2A) (12,14). Interestingly, Sll0933, a factor suggested to be involved in integration of CP47 into PSII subcomplexes, showed a different membrane localization (15).…”

Section: Pigments In Pdms Andmentioning

confidence: 99%

“…11). Thus, the cyanobacterial YidC/ Oxa1/Alb3 homolog Slr1471 has been shown to interact directly with the D1 protein during its integration into the membrane (12). Similarly, a direct interaction has been revealed between pD1 and YCF48, the Synechocystis homolog of HCF136 from Arabidopsis thaliana, which seems to be involved in facilitating formation of PSII RC intermediates (13,14).…”

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confidence: 93%

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An Intermediate Membrane Subfraction in Cyanobacteria Is Involved in an Assembly Network for Photosystem II Biogenesis

Rengstl

Oster

Stengel

et al. 2011

Journal of Biological Chemistry

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Early steps in the biogenesis of Photosystem II (PSII) in the cyanobacterium Synechocystis sp. PCC 6803 are thought to occur in a specialized membrane fraction that is characterized by the specific accumulation of the PSII assembly factor PratA and its interaction partner pD1, the precursor of the D1 protein of PSII. Here, we report the molecular characterization of this membrane fraction, called the PratA-defined membrane (PDM), with regard to its lipid and pigment composition and its association with PSII assembly factors, including YCF48, Slr1471, Sll0933, and Pitt. We demonstrate that YCF48 and Slr1471 are present and that the chlorophyll precursor chlorophyllide a accumulates in the PDM. Analysis of PDMs from various mutant lines suggests a central role for PratA in the spatial organization of PSII biogenesis. Moreover, quantitative immunoblot analyses revealed a network of interdependences between several PSII assembly factors and chlorophyll synthesis. In addition, formation of complexes containing both YCF48 and Sll0933 was substantiated by co-immunoprecipitation experiments. The findings are integrated into a refined model for PSII biogenesis in Synechocystis 6803.

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Section: Pigments In Pdms Andmentioning

confidence: 99%

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confidence: 93%

An Intermediate Membrane Subfraction in Cyanobacteria Is Involved in an Assembly Network for Photosystem II Biogenesis

Rengstl

Oster

Stengel

et al. 2011

Journal of Biological Chemistry

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“…LPA1 appears to be an integral membrane chaperone that assists efficient PSII assembly through direct interaction with D1 (Peng et al, 2006), and REP27 is essential for D1 protein turnover, permitting completion of the translation process, maturation, and activation of D1 into a functional PSII reaction center complex (Park et al, 2007). Ossenbü hl et al (2006) further found that Srl1471p, a homolog of ALB3, is essential for integrating the D1 precursor into the thylakoid membrane, leading to accumulation of the D1 precursor in the membrane phase.…”

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confidence: 99%

HCF243 Encodes a Chloroplast-Localized Protein Involved in the D1 Protein Stability of the Arabidopsis Photosystem II Complex

et al. 2011

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Numerous auxiliary nuclear factors have been identified to be involved in the dynamics of the photosystem II (PSII) complex. In this study, we characterized the high chlorophyll fluorescence243 (hcf243) mutant of Arabidopsis (Arabidopsis thaliana), which shows higher chlorophyll fluorescence and is severely deficient in the accumulation of PSII supercomplexes compared with the wild type. The amount of core subunits was greatly decreased, while the outer antenna subunits and other subunits were hardly affected in hcf243. In vivo protein-labeling experiments indicated that the synthesis rate of both D1 and D2 proteins decreased severely in hcf243, whereas no change was found in the rate of other plastid-encoded proteins. Furthermore, the degradation rate of the PSII core subunit D1 protein is higher in hcf243 than in the wild type, and the assembly of PSII is retarded significantly in the hcf243 mutant. HCF243, a nuclear gene, encodes a chloroplast protein that interacts with the D1 protein. HCF243 homologs were identified in angiosperms with one or two copies but were not found in lower plants and prokaryotes. These results suggest that HCF243, which arose after the origin of the higher plants, may act as a cofactor to maintain the stability of D1 protein and to promote the subsequent assembly of the PSII complex.PSII is a multisubunit protein-pigment complex embedded in the thylakoid membrane that harnesses light energy to split water into oxygen, protons, and electrons. It comprises more than 20 different subunits, most of which are integral membrane proteins and bind numerous cofactors (Wollman et al., 1999;Iwata and Barber, 2004;Nelson and Yocum, 2006). The PSII reaction center complex is composed of the D1 and D2 proteins, the a-and b-subunits of cytochrome b 559 , and the PsbI protein. The D1 and D2 heterodimers bind all the essential redox components of PSII required for primary charge separation and subsequent electron transfer (Nanba and Satoh, 1987). In addition, PSII core complexes also contain the intrinsic chlorophyll a-binding proteins (CP43 and CP47), the extrinsic oxygen-evolving complex (33-, 23-, and 17-kD proteins), and the other low-molecular-mass proteins (Bricker and Ghanotakis, 1996). The functional form of PSII in the thylakoid membrane consists of the PSII core and the associated light-harvesting complex (Nelson and Yocum, 2006).Despite considerable advances in the elucidation of the structure and function of PSII, knowledge of the assembly of this multiprotein complex is only in its infancy. A number of studies have proved that this assembly is likely to involve multistep processes (Rokka et al., 2005). The first step is formation of the PSII reaction center, in which the D1 protein is incorporated into a precomplex, probably consisting of the D2, cytochrome b 559 , and PsbI proteins (Adir et al., 1990;van Wijk et al., 1997;Mü ller and Eichacker, 1999;Zhang et al., 1999). Subsequently, CP47 and CP43, core antenna subunits that bind chlorophyll a, are recruited to form the PSII core compl...

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“…The protein Slr1471p (OXA1/Alb3/YidC homologous), for instance, has been shown to interact directly with the D1 protein during integration of the latter into the thylakoid membrane (8). The lumenal factor YCF48 (HCF136) is required for both efficient assembly and repair of PSII (9,10), and the 11-kDa lipoprotein Psb27 has been implicated in facilitating assembly of the manganese cluster of PSII (11,12).…”

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confidence: 99%

Interaction of the Periplasmic PratA Factor and the PsbA (D1) Protein during Biogenesis of Photosystem II in Synechocystis sp. PCC 6803

Schottkowski

Gkalympoudis

Tzekova

et al. 2009

Journal of Biological Chemistry

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The biogenesis of photosynthetic complexes is assisted by a growing number of trans-acting factors in both chloroplasts and cyanobacteria. We have previously shown that the periplasmic PratA factor from Synechocystis sp. PCC 6803 (Synechocystis 6803) is required for adequate C-terminal processing of the PsbA (D1) subunit of photosystem II (PSII) supporting the idea that the early steps of PSII assembly occur at the plasma membrane. Here we report on the molecular analysis of the interaction between PratA and the D1 protein. Both yeast two-hybrid and glutathione S-transferase pulldown assays revealed that PratA binds to the soluble forms of both mature and precursor D1 C-terminal regions. In agreement with that finding, the binding region was mapped to amino acid positions 314 -328 of D1 by applying a peptide-scanning approach. Approximately 10 -20% of the soluble PratA factor was found to be associated with membranes in a D1-dependent manner. Sucrose density gradient centrifugations allowed the identification of a specific membrane subfraction that contains both PratA and D1 and which might represent a transfer and/or connecting region between plasma and thylakoid membrane. Imaging data obtained with enhanced cyan fluorescent protein-labeled D1 protein in wild-type and pratA mutant backgrounds further supported this notion. Photosystem II (PSII)2 mediates water oxidation and initiates electron flow during light reactions of photosynthesis in cyanobacteria and in chloroplasts of eukaryotes. Cyanobacterial PSII has been characterized in great detail at the structural level (1-4). However, much less is known about the stepwise biogenesis of this molecular machine, which contains at least 19 protein subunits as well as a complex set of cofactors (5-7). In the prokaryotic model organism Synechocystis PCC sp. 6803 (hereafter Synechocystis 6803), several proteins have recently been identified that associate transiently with PSII, and inactivation of these leads to severe defects in PSII activity. Such proteins represent good candidates for putative assembly factors.The protein Slr1471p (OXA1/Alb3/YidC homologous), for instance, has been shown to interact directly with the D1 protein during integration of the latter into the thylakoid membrane (8). The lumenal factor YCF48 (HCF136) is required for both efficient assembly and repair of PSII (9, 10), and the 11-kDa lipoprotein Psb27 has been implicated in facilitating assembly of the manganese cluster of PSII (11, 12). Finally, the 22-kDa Psb29 protein is apparently necessary for accurate biogenesis of the inner antennae of PSII (13).We have previously shown that the tetratricopeptide repeat protein PratA is involved in the biogenesis of PSII: loss of PratA function affects the maturation of the reactioncenter protein D1 (14). In almost all photoautotrophic organisms, D1 is synthesized as a precursor with a C-terminal extension that must be removed to allow assembly of the manganese cluster at the lumenal side of PSII. In Synechocystis 6803, this extension consists of 16 ...

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The Synechocystis sp PCC 6803 Oxa1 Homolog Is Essential for Membrane Integration of Reaction Center Precursor Protein pD1

Cited by 52 publications

References 40 publications

An Intermediate Membrane Subfraction in Cyanobacteria Is Involved in an Assembly Network for Photosystem II Biogenesis

An Intermediate Membrane Subfraction in Cyanobacteria Is Involved in an Assembly Network for Photosystem II Biogenesis

HCF243 Encodes a Chloroplast-Localized Protein Involved in the D1 Protein Stability of the Arabidopsis Photosystem II Complex

Interaction of the Periplasmic PratA Factor and the PsbA (D1) Protein during Biogenesis of Photosystem II in Synechocystis sp. PCC 6803

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