A Novel Protein for Photosystem I Biogenesis

Stöckel, Jana; Oelmüller, Ralf

doi:10.1074/jbc.m309246200

Cited by 77 publications

(63 citation statements)

References 74 publications

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“…4) that the Ycf4 protein specifically functions in the biogenesis of PSI cores, we also investigated the accumulation of the PSI antenna proteins LhcA1, LhcA2, and LhcA4 using specific antibodies. LhcA proteins have been shown to accumulate independently of the PSI reaction center (Stöckel and Oelmüller, 2004;Stöckel et al, 2006). In contrast to all PSI core subunits tested, accumulation of the three proteins of the PSI antenna (LHCI) was unaffected in the transplastomic Dycf4 lines (and, as expected, also in the KD-psaA control mutant; Fig.…”

Section: Accumulation Of Thylakoid Protein Complexes In Dycf4 Plantsmentioning

confidence: 85%

“…As phylloquinone is a cofactor required only in PSI, mutants in phylloquinone biosynthesis show a specific deficiency in PSI accumulation (Lohmann et al, 2006). An example for a gene involved in cofactor insertion is Hcf101, which encodes a scaffold protein for [4Fe-4S] cluster assembly (Stöckel and Oelmüller, 2004;Schwenkert et al, 2010). A few proteins have been implicated in the assembly of the PSI protein subunits.…”

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confidence: 99%

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The Plastid Genome-Encoded Ycf4 Protein Functions as a Nonessential Assembly Factor for Photosystem I in Higher Plants

et al. 2012

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Photosystem biogenesis in the thylakoid membrane is a highly complicated process that requires the coordinated assembly of nucleus-encoded and chloroplast-encoded protein subunits as well as the insertion of hundreds of cofactors, such as chromophores (chlorophylls, carotenoids) and iron-sulfur clusters. The molecular details of the assembly process and the identity and functions of the auxiliary factors involved in it are only poorly understood. In this work, we have characterized the chloroplast genome-encoded ycf4 (for hypothetical chloroplast reading frame no. 4) gene, previously shown to encode a protein involved in photosystem I (PSI) biogenesis in the unicellular green alga Chlamydomonas reinhardtii. Using stable transformation of the chloroplast genome, we have generated ycf4 knockout plants in the higher plant tobacco (Nicotiana tabacum). Although these mutants are severely affected in their photosynthetic performance, they are capable of photoautotrophic growth, demonstrating that, different from Chlamydomonas, the ycf4 gene product is not essential for photosynthesis. We further show that ycf4 knockout plants are specifically deficient in PSI accumulation. Unaltered expression of plastid-encoded PSI genes and biochemical analyses suggest a posttranslational action of the Ycf4 protein in the PSI assembly process. With increasing leaf age, the contents of Ycf4 and Y3IP1, another auxiliary factor involved in PSI assembly, decrease strongly, whereas PSI contents remain constant, suggesting that PSI is highly stable and that its biogenesis is restricted to young leaves.

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Section: Accumulation Of Thylakoid Protein Complexes In Dycf4 Plantsmentioning

confidence: 85%

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confidence: 99%

The Plastid Genome-Encoded Ycf4 Protein Functions as a Nonessential Assembly Factor for Photosystem I in Higher Plants

et al. 2012

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“…1. HCF101 was demonstrated to be involved in chloroplast [Fe-S] cluster metabolism (29,30). The CFD1, Npb35, and huNbp35 (formally Nubp1) proteins were demonstrated to be involved in cytoplasmic [Fe-S] cluster metabolism (31,32).…”

Section: Nifusvcyse1) Involved In the Biosynthesis Of [Fe-s] Clustersmentioning

confidence: 99%

Bacterial ApbC Protein Has Two Biochemical Activities That Are Required for in Vivo Function

Boyd

Sondelski

Downs

2009

Journal of Biological Chemistry

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Analysis of the metabolic network anchored to thiamine biosynthesis in S. enterica identified lesions in three non-isc or -suf loci that compromise Fe-S metabolism as follows: apbC, apbE, and rseC (17-21). This metabolic system was subsequently used to dissect a role for cyaY and gshA in [Fe-S] cluster metabolism (6,22,23). Of these, the apbC (mrp in E. coli) locus was identified as the predominant site of lesions that altered thiamine synthesis by disrupting [Fe-S] cluster metabolism (17,18).ApbC is a member of the ParA subfamily of proteins that have a wide array of functions, including electron transfer (24), initiation of cell division (25), and DNA segregation (26,27). Importantly, ATP hydrolysis is required for function of all well characterized members of this subfamily, and all members contain a "deviant" Walker A motif, which contains two lysine residues instead of one (GKXXXGK(S/T)) (28). ApbC has been shown to hydrolyze ATP (17).Recently, five proteins with a high degree of identity to ApbC have been shown to be involved in [Fe-S] cluster metabolism in eukaryotes. The sequence alignments of the central portion of these proteins and bacterial ApbC are shown in Fig. 1. HCF101 was demonstrated to be involved in chloroplast [Fe-S] cluster metabolism (29, 30). The CFD1, Npb35, and huNbp35 (formally Nubp1) proteins were demonstrated to be involved in cytoplasmic [Fe-S] cluster metabolism (31,32). Ind1 was demonstrated to be involved in the maturation of [Fe-S] clusters in the mitochondrial enzyme NADH:ubiquinone oxidoreductase (33). There is currently no report of any of these proteins hydrolyzing ATP.Biochemical analysis of ApbC indicated that it could bind and transfer [Fe-S] clusters to Saccharomyces cerevisiae apo-isopropylmalate isomerase (34). Additional genetic studies indicated that ApbC has a degree of functional redundancy with IscU, a known [Fe-S] cluster scaffolding protein (35,36).In this study we investigate the correlation between the biochemical properties of ApbC (i.e. ATPase activity, [Fe-S] cluster binding, and [Fe-S] cluster transfer rates) and the in vivo function of this protein. This is the first detailed kinetic analysis of ATP hydrolysis for a member of the ParA subfamily of deviant Walker A proteins and the first functional analysis of a member of the ever expanding family of ApbC/Nbp35 proteins. Data presented indicate that noncomplementing variants have distinct biochemical properties that place them in three distinct classes.

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“…Both MNP2 and HCF101 lack the conserved CxxC motif that is usually found in the C terminus of Mrp/NBP35 proteins. Mutants in high chlorophyll fluorescence (HCF)101 have been characterized in Arabidopsis and have a defect in the assembly of PSI, as well as instability of ferredoxin-thioredoxin reductase, but not ferredoxin (Lezhneva et al 2004;Stö ckel and Oelmü ller 2004). HCF101 has an extra domain at its N terminus, domain of unknown function (DUF)59 (pfam PF01883) not found in the other Mrp/NBP35-like proteins.…”

Section: Resultsmentioning

confidence: 99%

Genome Analysis of Chlamydomonas reinhardtii Reveals The Existence of Multiple, Compartmentalized Iron–Sulfur Protein Assembly Machineries of Different Evolutionary Origins

Godman

Balk

2008

Genetics

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The unicellular green alga Chlamydomonas reinhardtii is used extensively as a model to study eukaryotic photosynthesis, flagellar functions, and more recently the production of hydrogen as biofuel. Two of these processes, photosynthesis and hydrogen production, are highly dependent on iron-sulfur (Fe-S) enzymes. To understand how Fe-S proteins are assembled in Chlamydomonas, we have analyzed its recently sequenced genome for orthologs of genes involved in Fe-S cluster assembly. We found a total of 32 open reading frames, most single copies, that are thought to constitute a mitochondrial assembly pathway, mitochondrial export machinery, a cytosolic assembly pathway, and components for Fe-S cluster assembly in the chloroplast. The chloroplast proteins are also expected to play a role in the assembly of the H-cluster in ½FeFe-hydrogenases, together with the recently identified HydEF and HydG proteins. Comparison with the higher plant model Arabidopsis indicated a strong degree of conservation of Fe-S cofactor assembly pathways in the green lineage, the pathways being derived from different origins during the evolution of the photosynthetic eukaryote. As a haploid, unicellular organism with available forward and reverse genetic tools, Chlamydomonas provides an excellent model system to study Fe-S cluster assembly and its regulation in photosynthetic eukaryotes.

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A Novel Protein for Photosystem I Biogenesis

Cited by 77 publications

References 74 publications

The Plastid Genome-Encoded Ycf4 Protein Functions as a Nonessential Assembly Factor for Photosystem I in Higher Plants

The Plastid Genome-Encoded Ycf4 Protein Functions as a Nonessential Assembly Factor for Photosystem I in Higher Plants

Bacterial ApbC Protein Has Two Biochemical Activities That Are Required for in Vivo Function

Genome Analysis of Chlamydomonas reinhardtii Reveals The Existence of Multiple, Compartmentalized Iron–Sulfur Protein Assembly Machineries of Different Evolutionary Origins

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