PratA, a Periplasmic Tetratricopeptide Repeat Protein Involved in Biogenesis of Photosystem II in Synechocystis sp. PCC 6803

Klinkert, Birgit; Ossenbühl, Friedrich; Sikorski, Martha; Berry, Stephan; Eichacker, Lutz A.; Nickelsen, Jörg

doi:10.1074/jbc.m405393200

Cited by 77 publications

(104 citation statements)

References 34 publications

Supporting

Mentioning

100

Contrasting

Order By: Relevance

“…1A). This resembles the observations on the periplasmic protein PratA deletion mutant in Synechocystis (13,14). In this mutant, the levels of PSII proteins were reduced to about 25%, and the D1 precursor processing was hampered.…”

Section: Discussionsupporting

confidence: 85%

“…Our efforts to detect the interaction between Psb27-H2 and CtpA was unsuccessful (data not shown) because CtpA perturbed this two-hybrid system, which was also observed in (13). The possibility that LPA19 interacts with D1 was examined by protein overlay assays.…”

Section: Lpa19 Is a Psb27mentioning

confidence: 99%

“…Subsequent assembly steps involve the association of the intrinsic antenna proteins CP47/CP43, integration of the small subunits, and assembly of the water-splitting system (11,12). Recently, in several model organisms, a number of PSII assembly factors have been identified, such as PratA, Slr2013, Slr0286, Hcf136, Lpa1, and Lpa2 (13)(14)(15)(16)(17)(18)(19). A unique property of PSII is that the damage directed to it occurs at all light intensities (20).…”

mentioning

confidence: 99%

See 2 more Smart Citations

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

View full text Add to dashboard Cite

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).

show abstract

Section: Discussionsupporting

confidence: 85%

Section: Lpa19 Is a Psb27mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

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

View full text Add to dashboard Cite

show abstract

“…The outer membrane and PM form the cell envelope and delimit the periplasmic space, whereas TMs are localized within the cell and house the large pigment-protein complexes of the photosynthetic electron transfer chain, i.e. Photosystem (PS) II, PSI, the cytochrome b 6 f complex, and the ATP synthase (1). It is not clear whether direct connections exist between the different membrane systems and, in particular, where synthesis of TMs is initiated (2)(3)(4).…”

mentioning

confidence: 99%

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

Self Cite

View full text Add to dashboard Cite

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.

show abstract

“…The D1 protein, which is directly involved in electron donor and acceptor site formation, is the most sensitive component of PSII since it is highly susceptible to light-induced damage (Aro et al, 1993). A number of proteins, such as the FtsH2 protease, the products of slr2013 and slr0286, as well as PratA, a periplasmic tetratricopeptide repeat protein, are involved in turnover of PSII in oxygenic phototrophic organisms (Klinkert et al, 2004;Komenda et al, 2006;Kufryk & Vermaas, 2003;Silva et al, 2003). The mechanism regulating the biogenesis and assembly of the PSII apparatus is still poorly understood and a specific function of N-terminal processing has so far not been described.…”

Section: Introductionmentioning

confidence: 99%

An alternative methionine aminopeptidase, MAP-A, is required for nitrogen starvation and high-light acclimation in the cyanobacterium Synechocystis sp. PCC 6803

2009

View full text Add to dashboard Cite

Methionine aminopeptidases (MetAPs or MAPs, encoded by map genes) are ubiquitous and pivotal enzymes for protein maturation in all living organisms. Whereas most bacteria harbour only one map gene, many cyanobacterial genomes contain two map paralogues, the genome of Synechocystis sp. PCC 6803 even three. The physiological function of multiple map paralogues remains elusive so far. This communication reports for the first time differential MetAP function in a cyanobacterium. In Synechocystis sp. PCC 6803, the universally conserved mapC gene (sll0555) is predominantly expressed in exponentially growing cells and appears to be a housekeeping gene. By contrast, expression of mapA (slr0918) and mapB (slr0786) genes increases during stress conditions. The mapB paralogue is only transiently expressed, whereas the widely distributed mapA gene appears to be the major MetAP during stress conditions. A mapA-deficient Synechocystis mutant shows a subtle impairment of photosystem II properties even under non-stressed conditions. In particular, the binding site for the quinone QB is affected, indicating specific N-terminal methionine processing requirements of photosystem II components. MAP-A-specific processing becomes essential under certain stress conditions, since the mapA-deficient mutant is severely impaired in surviving conditions of prolonged nitrogen starvation and high light exposure.

show abstract

PratA, a Periplasmic Tetratricopeptide Repeat Protein Involved in Biogenesis of Photosystem II in Synechocystis sp. PCC 6803

Cited by 77 publications

References 34 publications

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

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

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

An alternative methionine aminopeptidase, MAP-A, is required for nitrogen starvation and high-light acclimation in the cyanobacterium Synechocystis sp. PCC 6803

Contact Info

Product

Resources

About