Photosystem I in Cyanobacteria

Golbeck, John H.

doi:10.1007/0-306-48205-3_10

Cited by 14 publications

(23 citation statements)

References 161 publications

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“…PsaC is a 8Fe ferredoxin homolog found as a part of photosystem I and carries two [4Fe-4S] 2ϩ,1ϩ clusters, namely centers F A and F B , which serve as an electron donor to another FeS center, F x (59 -62). The redox potentials of the centers F A and F B of PsaC are both well below Ϫ500 mV (59), as in the cases reported for a lower potential [4Fe-4S] 2ϩ,1ϩ cluster (cluster II) of archaeal zinc-containing ferredoxins (6,12,63).…”

Section: Sequence and Xas Of Archaeal Zinc-containing Ferredoxinsupporting

confidence: 77%

Structural Conservation of the Isolated Zinc Site in Archaeal Zinc-containing Ferredoxins as Revealed by X-ray Absorption Spectroscopic Analysis and Its Evolutionary Implications

Cosper

Stålhandske

Iwasaki

et al. 1999

Journal of Biological Chemistry

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The zfx gene encoding a zinc-containing ferredoxin from Thermoplasma acidophilum strain HO-62 was cloned and sequenced. It is located upstream of two genes encoding an archaeal homolog of nascent polypeptide-associated complex ␣ subunit and a tRNA nucleotidyltransferase. This gene organization is not conserved in several euryarchaeoteal genomes. The multiple sequence alignments of the zfx gene product suggest significant sequence similarity of the ferredoxin core fold to that of a low potential 8Fe-containing dicluster ferredoxin without a zinc center. The tightly bound zinc site of zinc-containing ferredoxins from two phylogenetically distantly related Archaea, T. acidophilum HO-62 and Sulfolobus sp. strain 7, was further investigated by x-ray absorption spectroscopy. The zinc K-edge x-ray absorption spectra of both archaeal ferredoxins are strikingly similar, demonstrating that the same zinc site is found in T. acidophilum ferredoxin as in Sulfolobus sp. ferredoxin, which suggests the structural conservation of isolated zinc binding sites among archaeal zinc-containing ferredoxins. The sequence and spectroscopic data provide the common structural features of the archaeal zinc-containing ferredoxin family.

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Section: Sequence and Xas Of Archaeal Zinc-containing Ferredoxinsupporting

confidence: 77%

Structural Conservation of the Isolated Zinc Site in Archaeal Zinc-containing Ferredoxins as Revealed by X-ray Absorption Spectroscopic Analysis and Its Evolutionary Implications

Cosper

Stålhandske

Iwasaki

et al. 1999

Journal of Biological Chemistry

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“…PsaC and PsaD) are essential for PSI photochemistry (Bryant 1992;Golbeck 1992Golbeck , 1994. The PsaA and PsaB subunits, encoded by the psaA and psaB genes, are believed to associate with the essential electron transport cofactors P700, A0, A1 and Fx to carry out the light-dependent charge separation and charge stabilization.…”

mentioning

confidence: 99%

“…These subunits additionally are believed to harbor most of the approximately 100 Chl a molecules and 12-15/3-carotene molecules that play a role(s) in light-energy harvesting. PsaC harbors two [4Fe-4S] clusters, denoted FA and FB, that serve as the terminal electron acceptors for PS I (see Golbeck 1992Golbeck , 1994. PsaD stabilizes the association of PsaC with the PSI reaction center core (Li et al 1991b) and may also play a role in the binding of the soluble electron acceptors ferredoxin or flavodoxin (Wynn et al 1989).…”

mentioning

confidence: 99%

Characterization of a Synechococcus sp. strain PCC 7002 mutant lacking Photosystem I. Protein assembly and energy distribution in the absence of the Photosystem I reaction center core complex

Shen

Bryant

1995

Photosynth Res

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A Synechococcus sp. strain PCC 7002 ΔpsaAB::cat mutant has been constructed by deletional interposon mutagenesis of the psaA and psaB genes through selection and segregation under low-light conditions. This strain can grow photoheterotrophically with glycerol as carbon source with a doubling time of 25 h at low light intensity (10 μE m(-2) s(-1)). No Photosystem I (PS I)-associated chlorophyll fluorescence emission peak was detected in the ΔpsaAB::cat mutant. The chlorophyll content of the ΔpsaAB::cat mutant was approximately 20% that of the wild-type strain on a per cell basis. In the absence of the PsaA and PsaB proteins, several other PS I proteins do not accumulate to normal levels. Assembly of the peripheral PS I proteins PsaC,PsaD, PsaE, and PsaL is dependent on the presence of the PsaA and PsaB heterodimer core. The precursor form of PsaF may be inserted into the thylakoid membrane but is not processed to its mature form in the absence of PsaA and PsaB. The absence of PS I reaction centers has no apparent effect on Photosystem II (PS II) assembly and activity. Although the mutant exhibited somewhat greater fluorescence emission from phycocyanin, most of the light energy absorbed by phycobilisomes was efficiently transferred to the PS II reaction centers in the absence of the PS I. No light state transition could be detected in the ΔpsaAB::cat strain; in the absence of PS I, cells remain in state 1. Development of this relatively light-tolerant strain lacking PS I provides an important new tool for the genetic manipulation of PS I and further demonstrates the utility of Synechococcus sp. PCC 7002 for structural and functional analyses of the PS I reaction center.

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“…it mediates the light-driven electron transport from plastocyanin (or cytochrome c in some species) to ferredoxin (or flavodoxin) (Scheller et al, 2001). The subunits are named according to their genes, PsaA to PsaX (Golbeck, 1994;Chitnis, 1996;Fromme et al, 2001). In higher plants, the gene (PsaL) encoding polypeptide for subunit XI of photosystem I reaction center (PSI) is located in the nucleus (Ikeuchi and Inoue, 1991;Flieger et al, 1993;Scheller et al, 2001;Jensen et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

Identification and expression profiling of CLCuV-responsive transcripts in upland cotton (Gossypium hirsutum L.)

Aftab¹,

Shahid²,

Riaz³

et al. 2014

Turk J Biol

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CLCuV is one of the most serious causes of cotton damage for which no adequate remedy is available. The possible solution to this problem may be the transfer of resistant genes into the background of agronomical CLCuV-tolerant varieties. In response to viral infection, several plants may show qualitative and quantitative variations in gene expression. To study gene expression between diseased and tolerant plants, DDRT-PCR was performed. Upregulated gene expression was observed among cDNA transcripts screened through random primers. Seven transcripts have significant homology with known proteins (ribosomal protein, photosystem protein unit, membrane protein, and a predicted hypothetical protein). Quantitative real-time PCR showed varied levels of expression in tolerant as compared to CLCuV-diseased leaf samples. The potential candidate transcript DET1 was generated full length as GhLCVR. The deduced amino acid sequence, with a molecular mass of 16.1 kDa, contains a single open reading frame of 142 amino acids. The predicted amino acid sequence shares 33%-80% identities with Glycine max, Populus trichocarpa, Vitis vinifera, Zea mays, Ricinus communis, Arabidopsis thaliana, Picea sitchensis, Physcomitrella patens, and Staphylococcus aureus in descending order. This gene and other identified DETs could provide a valuable resource for the future improvement of cotton varieties against CLCuV infection.

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Photosystem I in Cyanobacteria

Cited by 14 publications

References 161 publications

Structural Conservation of the Isolated Zinc Site in Archaeal Zinc-containing Ferredoxins as Revealed by X-ray Absorption Spectroscopic Analysis and Its Evolutionary Implications

Structural Conservation of the Isolated Zinc Site in Archaeal Zinc-containing Ferredoxins as Revealed by X-ray Absorption Spectroscopic Analysis and Its Evolutionary Implications

Characterization of a Synechococcus sp. strain PCC 7002 mutant lacking Photosystem I. Protein assembly and energy distribution in the absence of the Photosystem I reaction center core complex

Identification and expression profiling of CLCuV-responsive transcripts in upland cotton (Gossypium hirsutum L.)

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