A Cytoplasmically Inherited Barley Mutant Is Defective in Photosystem I Assembly Due to a Temperature-Sensitive Defect in <i>ycf3</i> Splicing

Landau, Alejandra; Lokstein, Heiko; Scheller, Henrik Vibe; Láinez, Verónica; Maldonado, Sara; Prina, Alberto R.

doi:10.1104/pp.109.147843

Cited by 34 publications

(30 citation statements)

References 47 publications

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“…In a temperature-sensitive barley mutant in which ycf3 mRNA is impaired at high temperature, PSI accumulation is also affected. In this barley mutant, the reduction in PSI is related to the decrease in YCF3 protein content at different temperatures [41]. Thus, it appears that YCF3 may mediate a rate-limiting step in PSI assembly.…”

Section: Regulatory Factors For Psi Assemblymentioning

confidence: 97%

Regulatory factors for the assembly of thylakoid membrane protein complexes

Chi

Zhang

2012

Phil. Trans. R. Soc. B

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Major multi-protein photosynthetic complexes, located in thylakoid membranes, are responsible for the capture of light and its conversion into chemical energy in oxygenic photosynthetic organisms. Although the structures and functions of these photosynthetic complexes have been explored, the molecular mechanisms underlying their assembly remain elusive. In this review, we summarize current knowledge of the regulatory components involved in the assembly of thylakoid membrane protein complexes in photosynthetic organisms. Many of the known regulatory factors are conserved between prokaryotes and eukaryotes, whereas others appear to be newly evolved or to have expanded predominantly in eukaryotes. Their specific features and fundamental differences in cyanobacteria, green algae and land plants are discussed.

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Section: Regulatory Factors For Psi Assemblymentioning

confidence: 97%

Regulatory factors for the assembly of thylakoid membrane protein complexes

Chi

Zhang

2012

Phil. Trans. R. Soc. B

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“…Our findings suggest a new hypothesis to explain the LHC1/NDH defects in apo1 mutants: perhaps Ycf3 is necessary to assemble the PSI/NDH supercomplex, and in the absence of Ycf3, the LHC1 and NDH proteins become unstable. Analysis of psaA/B mRNA translation and NDH and LHC1 protein levels in ycf3 mutants (Ruf et al, 1997;Landau et al, 2009) can be used to address whether Ycf3 indeed plays these unanticipated roles. The reduced splicing of the clpP mRNA may also contribute to the protein defects in apo1 mutants, as the Clp protease complex plays wide-ranging roles in chloroplast biogenesis and homeostasis (Kim et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

“…The ycf3-int2 splicing defect was observed also in a second mutant allele of APO1 (apo1-2 in Figure 1C), confirming that the splicing defect is due to the disruption of APO1. Given that deletion of ycf3 results in the loss of PSI (Boudreau et al, 1997;Ruf et al, 1997;Landau et al, 2009), this splicing defect is sufficient to account for the absence of PSI in apo1 mutants.…”

Section: Apo1 Is Required For Ycf3-int2 Splicingmentioning

confidence: 99%

APO1 Promotes the Splicing of Chloroplast Group II Introns and Harbors a Plant-Specific Zinc-Dependent RNA Binding Domain

et al. 2011

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Arabidopsis thaliana APO1 is required for the accumulation of the chloroplast photosystem I and NADH dehydrogenase complexes and had been proposed to facilitate the incorporation of [4Fe-4S] clusters into these complexes. The identification of maize (Zea mays) APO1 in coimmunoprecipitates with a protein involved in chloroplast RNA splicing prompted us to investigate a role for APO1 in splicing. We show here that APO1 promotes the splicing of several chloroplast group II introns: in Arabidopsis apo1 mutants, ycf3-intron 2 remains completely unspliced, petD intron splicing is strongly reduced, and the splicing of several other introns is compromised. These splicing defects can account for the loss of photosynthetic complexes in apo1 mutants. Recombinant APO1 from both maize and Arabidopsis binds RNA with high affinity in vitro, demonstrating that DUF794, the domain of unknown function that makes up almost the entirety of APO1, is an RNA binding domain. We provide evidence that DUF794 harbors two motifs that resemble zinc fingers, that these bind zinc, and that they are essential for APO1 function. DUF794 is found in a plant-specific protein family whose members are all predicted to localize to mitochondria or chloroplasts. Thus, DUF794 adds a new example to the repertoire of plant-specific RNA binding domains that emerged as a product of nuclear-organellar coevolution.

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“…Some of the available PsaA/B mutants are either defective in the transcription of the psaA-psaB-rps14 operon (Hein et al, 2009) or in its stability ; others are impaired in the translation of the dimeric complex or cannot accumulate a stable heterodimer (Stöckel et al, 2006;Albus et al, 2010) or are affected in intron splicing of chloroplast mRNAs, including those encoding molecular chaperone-like complexes, such as Ycf3 (Landau et al, 2009;Ye et al, 2012); others are defective in the stable assembly of several [4Fe-4S] cluster-containing complexes of chloroplasts, including the PsaA/ B dimer (Schwenkert et al, 2010).…”

Section: Comparison Between Nox and Other Mutants Affected In The Biomentioning

confidence: 99%

The Arabidopsis nox Mutant Lacking Carotene Hydroxylase Activity Reveals a Critical Role for Xanthophylls in Photosystem I Biogenesis

et al. 2013

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Carotenes, and their oxygenated derivatives xanthophylls, are essential components of the photosynthetic apparatus. They contribute to the assembly of photosynthetic complexes and participate in light absorption and chloroplast photoprotection. Here, we studied the role of xanthophylls, as distinct from that of carotenes, by characterizing a no xanthophylls (nox) mutant of Arabidopsis thaliana, which was obtained by combining mutations targeting the four carotenoid hydroxylase genes. nox plants retained a-and b-carotenes but were devoid in xanthophylls. The phenotype included depletion of light-harvesting complex (LHC) subunits and impairment of nonphotochemical quenching, two effects consistent with the location of xanthophylls in photosystem II antenna, but also a decreased efficiency of photosynthetic electron transfer, photosensitivity, and lethality in soil. Biochemical analysis revealed that the nox mutant was specifically depleted in photosystem I function due to a severe deficiency in PsaA/B subunits. While the stationary level of psaA/B transcripts showed no major differences between genotypes, the stability of newly synthesized PsaA/B proteins was decreased and translation of psaA/B mRNA was impaired in nox with respect to wild-type plants. We conclude that xanthophylls, besides their role in photoprotection and LHC assembly, are also needed for photosystem I core translation and stability, thus making these compounds indispensable for autotrophic growth.

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A Cytoplasmically Inherited Barley Mutant Is Defective in Photosystem I Assembly Due to a Temperature-Sensitive Defect in ycf3 Splicing

Cited by 34 publications

References 47 publications

Regulatory factors for the assembly of thylakoid membrane protein complexes

Regulatory factors for the assembly of thylakoid membrane protein complexes

APO1 Promotes the Splicing of Chloroplast Group II Introns and Harbors a Plant-Specific Zinc-Dependent RNA Binding Domain

The Arabidopsis nox Mutant Lacking Carotene Hydroxylase Activity Reveals a Critical Role for Xanthophylls in Photosystem I Biogenesis

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