A cDNA clone encoding a 10.8 kDa photosystem I polypeptide of barley

Okkels, Jens Sigurd; Jepsen, Lars Bæk; Hønberg, Lisbeth Skou; Lehmbeck, Jan; Scheller, Henrik Vibe; Brandt, Peter; Høyer‐Hansen, Gunilla; Stummann, Bjarne M.; Henningsen, Knud W.; Wettstein, Diter von; Møller, Birger Lindberg

doi:10.1016/0014-5793(88)80181-9

Cited by 55 publications

(21 citation statements)

References 36 publications

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“…6. Similarity between NH2-terminal regions of barley PSI-N and PSI-E and H. The amino acid sequences of PSI-E, and H were determined by [ 19,22]. Identical residues (solid line) and conservative substitutions (dotted line) are boxed.…”

Section: Discussionmentioning

confidence: 99%

“…The primary structure of most of the PSI subunits has been determined and most have been sequenced for barley [12,19,20,22,23,27]. Cross-linking, antibody inhibition and reconstitution studies have shown that PSI-D and PSI-E The nucleotide sequence data reported will appear in the EMBL, Genbank and DDBJ Nucleotide Sequence Databases under the accession number X66428.…”

Section: Introductionmentioning

confidence: 99%

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The primary structure of a cDNA for PsaN, encoding an extrinsic lumenal polypeptide of barley photosystem I

Knoetzel

Simpson

1993

Plant Mol Biol

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A cDNA clone encoding a 15,501 Da photosystem I (PSI) subunit of barley was isolated using an oligonucleotide based on the NH2-terminal amino acid sequence of the isolated protein. The polypeptide, which migrates with an apparent molecular mass of 9.5 kDa on denaturing SDS-PAGE, has been designated PSI-N, and the corresponding gene is PsaN. Analysis of the deduced protein sequence indicates a mature protein of 85 amino acid residues and a molecular mass of 9818 Da. PSI-N is a hydrophilic, extrinsic protein with no predicted membrane-spanning regions. The transit peptide of 60 residues (5683 Da) contains a predicted hydrophobic alpha-helix, suggesting that the protein is routed into the thylakoid lumen. Thus, PSI-N is the second known lumenal protein component associated with PSI, together with PSI-F.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The primary structure of a cDNA for PsaN, encoding an extrinsic lumenal polypeptide of barley photosystem I

Knoetzel

Simpson

1993

Plant Mol Biol

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“…Subunit IV, the product of the psaE gene, is also thought to be located on the stroma side of the thylakoids. It has been described in different higher plants [6,9] and Chlamydomonas [ …”

Section: Introductionmentioning

confidence: 99%

Amino acid sequence of photosystem I subunit IV from the cyanobacterium Synechocystis PCC 6803

Rousseau

Lagoutte

1990

FEBS Letters

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We describe here the complete amino acid sequence of photosystem I subunit IV from Synechocystis 6803. The molecular mass of 8.0 kDa is lower than in higher plants and Chlamydomonas, due to the lack of a characteristic, proline-rich, N-terminal sequence. The remaining sequence exhibits a good conservation, with a hydrophilic and strongly basic N-terminal head followed by two hydrophobic domains. There is no possibility of classical membrane-spanning alpha helices. This component is likely to be one of the most stroma accessible subunits of photosystem I.

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“…In cyanobacteria, however, neither a protein nor a gene corresponding to the iron-sulfur center-carrying component has been identified yet, although there are many functional and molecular biological indications of its presence [12][13][14]. The other core components of higher plants so far sequenced are all encoded by nuclear genome and their sequences vary considerably among plant species [15][16][17][18][19][20]. Some such core components from cyanobacteria have been also sequenced, but only one component has been proven to correspond to a higher plant homologue (subunit II or psaD product) [4,21,22].…”

Section: Introductionmentioning

confidence: 99%

Identification of photosystem I components from the cyanobacterium, Synechococcus vulcanus by N‐terminal sequencing

et al. 1989

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The photosystem I core complex isolated from a thermophilic cyanobacterium, Synechococcus vulcanus, is composed of eight low-molecular-mass proteins of 18, 14, 12, 9.5, 9, 6.5, 5 and 4.1 kDa in addition to the PSI chlorophyll protein. N-terminal amino acid sequences of all these components were determined and compared with those of higher plants. Clearly, the 9.5 kDa component corresponds to the protein which carries the non-berne iron-sulfur centers A and B. This protein is so poorly visualized by staining that it has probably been overlooked in gel electrophoresis analyses. The 18, 14, 12 and 9 kDa components show appreciable homology with respective subunits of higher plant PS I. In contrast, the 6.5, 5 and 4.1 kDa components do not correspond to any known proteins except that the sequence of the 4.1 kDa component matches an unidentified open reading frame (ORF) 42 (liverwort) or ORF44 (tobacco) of chloroplast DNA.

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A cDNA clone encoding a 10.8 kDa photosystem I polypeptide of barley

Cited by 55 publications

References 36 publications

The primary structure of a cDNA for PsaN, encoding an extrinsic lumenal polypeptide of barley photosystem I

The primary structure of a cDNA for PsaN, encoding an extrinsic lumenal polypeptide of barley photosystem I

Amino acid sequence of photosystem I subunit IV from the cyanobacterium Synechocystis PCC 6803

Identification of photosystem I components from the cyanobacterium, Synechococcus vulcanus by N‐terminal sequencing

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