A cDNA clone encoding the precursor for a 10.2 kDa photosystem I polypeptide of barley

Okkels, Jens Sigurd; Scheller, Henrik Vibe; Jepsen, Lars Bæk; Møller, Birger Lindberg

doi:10.1016/0014-5793(89)80799-9

Cited by 40 publications

(11 citation statements)

References 36 publications

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“…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%

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: 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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“…The DNA constructs used in this study were pBluescript plasmids containing cDNA inserts encoding the precursors of barley PSI-H [15], barley PSI-L [17], and barley PSI-G (this paper). Preparation of the radiolabelled precursors and the import assays were performed essentially according to Dahlin and Cline [4].…”

Section: Methodsmentioning

confidence: 99%

“…Twelve different protein subThe nucleotide sequence data reported will appear in the EMBL, GenBank and DDBJ nucleotide sequence databases under the accession number X60t58. units have been identified in PSI core complexes and their primary structure have been determined from different species (for recent reviews see [1,31. In higher plants and algae five of the subunits are chloroplast-encoded (PSI-A, -B, -C, -I, -J) and seven are nuclear-encoded (PSI-D, -E, -F, -G,-H, -K, -L) using a designation of the subunits according to their corresponding genes psaA to PsaL, where in barley psa indicates a chloroplast gene and Psa indicates a nuclear gene [9,15]. Previously no sequence similarity between the nuclear-encoded subunits have been reported except for the N-terminal part of barley PSI-D and PSI-E [19].…”

Section: Introductionmentioning

confidence: 99%

A cDNA clone from barley encoding the precursor from the photosystem I polypeptide PSI-G: Sequence similarity to PSI-K

Okkels¹,

Nielsen²,

Scheller³

et al. 1992

Plant Mol Biol

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A cDNA clone encoding the photosystem I subunit, PSI-G was isolated from barley using an oligonucleotide specifying a partial amino acid sequence from a 9 kDa polypeptide of barley photosystem I. The 724 bp sequence contains an open reading frame encoding a precursor polypeptide of 15,107 kDa. Import studies using the in vitro expressed barley PsaG cDNA clone demonstrate that PSI-G migrates with an apparent molecular mass of 9 kDa on SDS-polyacrylamide gels together with PSI-C (subunit-VII). The previous assignment of the gene product of PsaG from spinach as subunit V (Steppuhn J, Hermans J, Nechushtai R, Ljungberg U, Thümmler F, Lottspeich F, Herrmann RG, FEBS Lett 237: 218-224, 1988) needs to be re-examined. The expression of the psaG gene is light-induced similar to other barley photosystem I genes. A significant sequence similarity to PSI-K from Chlamydomonas reinhardtii was discovered when a gene database was searched with the barley PSI-G amino acid sequence. Extensive sequence similarity between the nuclear-encoded photosystem I subunits has not previously been found. The observed sequence similarity between PSI-G and PSI-K suggests a symmetric location of these subunits in the photosystem I complex. The hydropathy plot of the barley PSI-G polypeptide indicates two membrane-spanning regions which are also found at the corresponding locations in the PSI-K polypeptide. PSI-G and PSI-K probably have evolved from a gene duplication of an ancestral gene.

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“…Recently it became clear that gene GOS5 corresponds with the barley gene psaH encoding a 9.5 kDa photosystem I polypeptide [42]. The single-copy rice gene contains two intron sequences (125 and 77 nucleotides; Fig.…”

Section: Introductionmentioning

confidence: 99%

Transient and stable expression of gusA fusions with rice genes in rice, barley and perennial ryegrass

et al. 1993

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Transcriptional and translational fusions were made between the reading frame coding for beta-D-glucuronidase and sequences of either a constitutively expressed rice gene (GOS2) involved in initiation of translation or a light-inducible rice gene (GOS5). The transient expression of the fusions was studied via particle bombardment of seedling tissues of rice, perennial ryegrass and barley. Furthermore, the results of transient and stable expression were compared for cell suspensions of four rice varieties, one barley variety and one perennial ryegrass variety. The GOS2-gusA fusions were active in all three monocots studied. Best results were obtained for a construct having both a transcriptional and a translational fusion as well as intron and exon sequences (PORCEHyg). The level of GUS activity was in the range of activities as obtained by the 35S CaMV promoter transcriptionally fused to gusA. The gusA fusion with the light-inducible gene (GOS5) was active in green seedling tissues of all monocots studied. Also a weak expression compared to the GOS2 constructs was found in stably transformed rice callus. The gusA fusions with the mannopine synthase promoters 1' and 2' of the TR-DNA were transiently expressed at lower levels in cell suspensions than PORCEHyg. For stably transformed rice callus the expression of the GOS2-gusA fusion often decreased during prolonged subculture. This decrease in GUS activity and the various GUS-staining phenotypes of transgenic calli are explained by the presence of different cell types in the suspensions used and in the calli. It is presumed that the nature of the cells and their relative contribution in the calli change drastically upon further subculture.

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A cDNA clone encoding the precursor for a 10.2 kDa photosystem I polypeptide of barley

Cited by 40 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

A cDNA clone from barley encoding the precursor from the photosystem I polypeptide PSI-G: Sequence similarity to PSI-K

Transient and stable expression of gusA fusions with rice genes in rice, barley and perennial ryegrass

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