The PsbP Domain Protein 1 Functions in the Assembly of Lumenal Domains in Photosystem I

Roose, Johnna L.; Frankel, Laurie K.; Bricker, Terry M.

doi:10.1074/jbc.m114.589085

Cited by 23 publications

(20 citation statements)

References 43 publications

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“…First, PPD1, like PSA2, localizes to the thylakoid lumen (9). Second, the accumulation of PsaG is especially sensitive to the partial loss of PPD1 (10). Finally, PPD1 is found in a complex that comigrates with the PSA2-PsaG complex in native gels (Fig.…”

Section: Discussionmentioning

confidence: 94%

“…This process necessitates the coordinated assembly of subunits and prosthetic groups at the thylakoid membrane where PSI is situated. Several factors have been described that are required for the assembly of PSI but that are not found in the mature complex; these include the chloroplast-encoded proteins Ycf3 and Ycf4 (4 -6) and the nucleus-encoded proteins Y3IP1 (7), Pyg7 (8), and PPD1 (9,10). Additional proteins mediate the association of prosthetic groups with PSI subunits (11)(12)(13)(14).…”

Section: Photosystem I (Psi)mentioning

confidence: 99%

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A Thylakoid Membrane Protein Harboring a DnaJ-type Zinc Finger Domain Is Required for Photosystem I Accumulation in Plants

Fristedt¹,

Williams‐Carrier

Merchant³

et al. 2014

Journal of Biological Chemistry

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Background: Photosystem I is a large protein/pigment assembly required for photosynthesis. Results: The PSA2 protein harbors a DnaJ-type zinc finger domain, is required for Photosystem I accumulation, and is found in a PsaG-containing complex in the thylakoid lumen. Conclusion: PSA2 promotes Photosystem I biogenesis via interaction with a PsaG-containing complex in the thylakoid lumen. Significance: These findings elucidate the biogenesis of the photosynthetic apparatus.

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Section: Discussionmentioning

confidence: 94%

Section: Photosystem I (Psi)mentioning

confidence: 99%

A Thylakoid Membrane Protein Harboring a DnaJ-type Zinc Finger Domain Is Required for Photosystem I Accumulation in Plants

Fristedt¹,

Williams‐Carrier

Merchant³

et al. 2014

Journal of Biological Chemistry

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“…The PSI biosynthesis pathway is still rather poorly characterized (Schöttler et al, 2011). Even if the PSI-LHCI assembly steps remain elusive, several auxiliary proteins have been identified that transiently assist the biogenesis and assembly of PSI (for review, see Schöttler et al, 2011), and novel PSI assembly factors are discovered constantly (Liu et al, 2012;Fristedt et al, 2014;Roose et al, 2014).…”

mentioning

confidence: 99%

FtsH facilitates proper biosynthesis of photosystem I in Arabidopsis thaliana

Järvi¹,

Suorsa

Tadini

et al. 2016

Plant Physiol.

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Thylakoid membrane-bound FtsH proteases have a well-characterized role in degradation of the photosystem II (PSII) reaction center protein D1 upon repair of photodamaged PSII. Here, we show that the Arabidopsis (Arabidopsis thaliana) var1 and var2 mutants, devoid of the FtsH5 and FtsH2 proteins, respectively, are capable of normal D1 protein turnover under moderate growth light intensity. Instead, they both demonstrate a significant scarcity of PSI complexes. It is further shown that the reduced level of PSI does not result from accelerated photodamage of the PSI centers in var1 or var2 under moderate growth light intensity. On the contrary, radiolabeling experiments revealed impaired synthesis of the PsaA/B reaction center proteins of PSI, which was accompanied by the accumulation of PSI-specific assembly factors. psaA/B transcript accumulation and translation initiation, however, occurred in var1 and var2 mutants as in wild-type Arabidopsis, suggesting problems in later stages of PsaA/B protein expression in the two var mutants. Presumably, the thylakoid membrane-bound FtsH5 and FtsH2 have dual functions in the maintenance of photosynthetic complexes. In addition to their function as a protease in the degradation of the photodamaged D1 protein, they also are required, either directly or indirectly, for early assembly of the PSI complexes.

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“…9). By contrast, PSA2 and another luminal PSI assembly factor, PPD1, are found in smaller complexes of approximately 350 kD (Fristedt et al, 2014;Roose et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

“…Ycf3, Ycf4, and Y3IP1 associate with the stromal face of the thylakoid membrane, and they have been suggested to participate in the assembly of the stromal ridge (Boudreau et al, 1997;Ruf et al, 1997;Ozawa et al, 2009;Albus et al, 2010;Krech et al, 2012). PPD1 and PSA2 associate with the lumenal face of the thylakoid membrane (Liu et al, 2012;Fristedt et al, 2014;Roose et al, 2014), whereas PYG7 is an integral membrane protein (Stöckel et al, 2006). A recent study of the PYG7 ortholog in Chlamydomonas reported that it is required for PSI biogenesis specifically in the presence of molecular oxygen, which led to a model in which PYG7 shields Fe-S clusters or the cysteines that bind them from oxidation during PSI assembly (Heinnickel et al, 2016).…”

mentioning

confidence: 99%

PSA3, a Protein on the Stromal Face of the Thylakoid Membrane, Promotes Photosystem I Accumulation in Cooperation with the Assembly Factor PYG7

2017

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PSI is a large protein-pigment complex located in the thylakoid membrane in cyanobacteria, plants, and algae. Although the structure and components of PSI are well characterized, mechanisms that orchestrate its assembly are poorly understood. In this study, we discovered a novel nucleus-encoded protein, Photosystem I Assembly3 (PSA3), that is required for PSI accumulation. PSA3 is conserved among green photosynthetic eukaryotes but is lacking in cyanobacteria. Mutations in the psa3 gene cause the specific loss of PSI in Arabidopsis (Arabidopsis thaliana) and maize (Zea mays). Ribosome profiling and pulse-labeling analyses showed that chloroplast-encoded PSI subunits are synthesized at normal rates in psa3 mutants, indicating that PSA3 is involved in the biogenesis of PSI at a posttranslational step. PSA3 resides on the stromal face of the thylakoid membrane, where it is found in a complex that is slightly smaller than PSI. Structural predictions suggest that PSA3 binds a basic peptide in a manner that is sensitive to the oxidation state of Cys pairs flanking the predicted peptide binding groove. PSA3 and the previously described PSI biogenesis factor PYG7 interact in yeast two-hybrid and bimolecular fluorescence complementation assays, and they are found in thylakoid membrane complexes of similar size. These and other results indicate that PSA3 cooperates with PYG7 to promote the stable assembly of PSI, and that the PsaC subunit is likely to be the primary target of their action.

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The PsbP Domain Protein 1 Functions in the Assembly of Lumenal Domains in Photosystem I

Cited by 23 publications

References 43 publications

A Thylakoid Membrane Protein Harboring a DnaJ-type Zinc Finger Domain Is Required for Photosystem I Accumulation in Plants

A Thylakoid Membrane Protein Harboring a DnaJ-type Zinc Finger Domain Is Required for Photosystem I Accumulation in Plants

FtsH facilitates proper biosynthesis of photosystem I in Arabidopsis thaliana

PSA3, a Protein on the Stromal Face of the Thylakoid Membrane, Promotes Photosystem I Accumulation in Cooperation with the Assembly Factor PYG7

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