Functional Studies of Ycf3

Naver, Helle; Boudreau, Eric; Rochaix, Jean‐David

doi:10.1105/tpc.010253

Cited by 61 publications

(14 citation statements)

References 57 publications

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“…IEF in the first dimension excludes some integral membrane proteins as a result of poor solubility in the neutral or zwitterionic detergents that must be used in IEF [41,42]. Although addition of amidosulfobetaine detergents along with thiourea [43][44][45] as well as addition of DM [46] have increased protein separation in some cases, attempts to use this approach for a complete proteomic analysis of thylakoids have not been productive, to date. Hippler and coworkers [19] reported the presence of highly hydrophobic PsaA in 2-D IEF/SDS-PAGE gels of thylakoid membrane from Chlamydomonas using DM, giving confidence that the larger integral proteins may be mapped, but most proteins from the PSII core complex were not revealed.…”

Section: Discussionmentioning

confidence: 99%

Retraction: A proteomic approach for investigation of photosynthetic apparatus in plants

Ciambella¹,

Roepstorff²,

Aro³

et al. 2005

Proteomics

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The proteome of the photosynthetic apparatus of barley (Hordeum vulgare), obtained by analysis of thylakoids without any previous fractionation, was mapped by native electrophoresis followed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) as the second dimension two-dimensional-blue native (2-D/BN)/SDS-PAGE). This protocol provided an excellent alternative to the 2-D-isoelectric focusing/sodium dodecyl sulfate-polyacrylamide gel electrophoresis for 2-D separation of the most hydrophobic thylakoid proteins. Monocots and dicots showed significant differences in the first dimension while in the second dimension patterns appeared similar. Identification of each spot was performed by internal peptide primary sequence determination using both nano-electrospray ionization tandem mass spectrometry and, to a lesser extent, peptide mass fingerprinting matrix-assisted laser desorption/ionization-time of flight using MALDI-TOF. This is due in particular to the fact that a limited number of peptides was obtained after trypsin digestion of these highly hydrophobic proteins. A larger number of peptides from hydrophilic intermembrane domains of transmembrane proteins were detected. Despite this, about 70% of the expected proteins were identified, including proteins with grand average of hydropathicity scores higher than 0.5. It is therefore reasonable to assert that protein hydrophobicity is not the limiting factor. Small proteins were not well identified with trypsin digestion. Instead some of these could be identified using acid hydrolysis. The method presented here does not require prefractionation of different thylakoid complexes and consequently gives confidence in comparing the proteome of the photosynthetic apparatus before and after treatment. It thus allows us to understand the molecular mechanisms underlying physiological adaptations of higher plants and to perform screening of photosynthetic mutants.

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Section: Discussionmentioning

confidence: 99%

Retraction: A proteomic approach for investigation of photosynthetic apparatus in plants

Ciambella¹,

Roepstorff²,

Aro³

et al. 2005

Proteomics

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“…Ycf3 contains three tetratrico-peptide repeats that are believed to function as sites for protein-protein interactions. Mutations in some of these tetratrico-peptide repeats lead to a modest decrease in PSI, but they prevent photo-autotrophic growth and lead to enhanced photosensitivity [23]. The latter can be relieved under anaerobic conditions, suggesting that it is caused by photo-oxidative damage.…”

Section: Mutants Deficient In Psi Assemblymentioning

confidence: 98%

“…A temperature-sensitive ycf3 mutant with changes near the N-terminal end of Ycf3 was used in temperature-shift experiments to show that Ycf3 is required for PSI assembly rather than for its stability. Moreover, Ycf3 was shown to interact directly and specifically with the PSI subunits PsaA and PsaD, but not with subunits of other photosynthetic complexes [23].…”

Section: Mutants Deficient In Psi Assemblymentioning

confidence: 99%

Post-transcriptional steps involved in the assembly of photosystem I in Chlamydomonas

Rochaix

Perron

Dauvillée

et al. 2004

Biochemical Society Transactions

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Assembly of the PSI (photosystem I) complex in eukaryotic photosynthetic organisms depends on the concerted interactions of the nuclear and chloroplast genetic systems. We have identified several nucleus-encoded factors of Chlamydomonas reinhardtii that are specifically required for the synthesis of the two large chloroplast-encoded reaction-centre polypeptides, PsaA and PsaB, of photosystem I and that function at plastid post-transcriptional steps. Raa1, Raa2 and Raa3 are required for the splicing of the three discontinuous psaA precursor transcripts; they are part of large RNA-protein complexes that are reminiscent of spliceosomal particles. Tab1 and Tab2 are involved in the initiation of translation of the psaB mRNA and are localized in the membrane and stromal phases of the chloroplast, where they are associated with high-molecular-mass complexes. Moreover, two chloroplast-encoded proteins, Ycf3 and Ycf4, are required for the primary steps of assembling the photosystem I subunits into a functional complex.

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“…Ycf3 contains three tetratricopeptide‐like domains that are thought to be involved in protein–protein interactions. A temperature‐sensitive ycf3 mutant of C. reinhardtii has been used in temperature shift experiments to show that Ycf3 is involved in the assembly, rather than in the stability of PSI [14]. Both Ycf3 and Ycf4 are located in the thylakoid membrane.…”

Section: Assembly Of Psimentioning

confidence: 99%

“…Although they do not cofractionate with PSI upon solubilization of the membrane with non‐ionic detergents, it is likely that they interact with some of the PSI subunits. Indeed, co‐immunoprecipitations of solubilized thylakoid membranes with antisera raised against several PSI subunits indicate that Ycf3 interacts with a restricted set of PSI subunits, in particular with PsaD [14]. Recent experiments using the bacterial two‐hybrid system have confirmed a direct interaction between PsaD and Ycf3 (D. Dauvillée and J.D.…”

Section: Assembly Of Psimentioning

confidence: 99%

Chlamydomonas, a model system for studying the assembly and dynamics of photosynthetic complexes

Rochaix

2002

FEBS Letters

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The green unicellular alga Chlamydomonas reinhardtii has emerged as a powerful model system for studying the biosynthesis of the photosynthetic apparatus and the acclimation of this system to changes in light conditions. The assembly of the photosynthetic complexes involves the coordinate interaction between the nuclear and chloroplast genetic systems. Many factors involved in speci¢c chloroplast post-transcriptional steps have been identi¢ed and characterized. Chlamydomonas is able to adapt to changes in light quality and in cellular ATP content by performing state transition, a process that leads to a redistribution of light excitation energy between photosystem II and photosystem I and that involves the redox state of the plastoquinone pool, the cytochrome b 6 f complex and one or several kinases speci¢c for the light-harvesting system. Genetic approaches have provided new insights into this process. ß 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

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Functional Studies of Ycf3

Cited by 61 publications

References 57 publications

Retraction: A proteomic approach for investigation of photosynthetic apparatus in plants

Retraction: A proteomic approach for investigation of photosynthetic apparatus in plants

Post-transcriptional steps involved in the assembly of photosystem I in Chlamydomonas

Chlamydomonas, a model system for studying the assembly and dynamics of photosynthetic complexes

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