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  • 1
    Electronic Resource
    Electronic Resource
    The gene for the Mr 10,000 phosphoprotein associated with photosystem II is part of the psbB operon of the spinach plastid chromosome (1986)
    Springer
    Current genetics 11 (1986), S. 165-169 
    Details
    ISSN: 1432-0983
    Keywords: Photosystem II gene ; Phosphoprotein ; Plastid DNA ; Polycistronic transcription ; Spinach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We present the nucleotide and derived amino acid sequence of the gene for the 10 kd phosphoprotein associated with photosystem II. This gene was identified by comparing the recently published first nine amino acid residues for the 10 kd phosphoprotein of spinach (Farchaus and Dilley 1986) with available sequence data from the spinach plastid chromosome. The gene, designated psbH, is part of an operon that encodes the 51 kd chlorophyll a apoprotein of the photosystem II reaction center (psbB), the phosphoprotein (73 codons), cytochrome b6 (petB) and subunit IV (petD) of the cytochrome b/f complex in the order given. Northern blot analysis revealed a complex in vivo RNA pattern for this DNA segment resulting from an extensive modification of a 5.6 kb long putative primary transcript which includes a monocistronic RNA species for the phosphoprotein of approximately 420 bases. The deduced amino acid sequence for the phosphoprotein indicates a polypeptide corresponding to a molecular weight of 7.8 kb. Secondary structure predictions place all potential phosphorylation sites on the stromal side of the membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00420602
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  • 2
    Electronic Resource
    Electronic Resource
    Localization and nucleotide sequence of the gene for the ATP synthase proteolipid subunit on the spinach plastid chromosome (1983)
    Springer
    Current genetics 7 (1983), S. 129-138 
    Details
    ISSN: 1432-0983
    Keywords: ATP synthase proteolipid subunit ; Plastid DNA ; Gene mapping ; Nucleotide sequence ; Spinach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A 1.6 kbp DNA segment of spinach plastid DNA has been shown to carry the gene for the proteolipid subunit of the ATP synthase. Each plastid chromosome contains one copy of this gene which is located in the large single-copy region of the chromosome near that of the ATP synthase alpha subunit. These two genes are transcribed in the same direction and probably in distinct RNA species. The proteolipid gene was located by hybrid-selection mapping, by transcription/translation of recombinant DNAs and by nucleotide sequencing. The in vitro product was identified by electrophoretic criteria including its characteristic shift in electrophoretic mobility upon incubation with dicyclohexylcarbodiimide, and immunology. The nucleotide sequence of the proteolipid gene is uninterrupted. The deduced amino acid sequence coincides with the published amino acid sequence for this protein and shows little homology with the published sequence of the proteolipid subunit of E. coli.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00365638
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  • 3
    Electronic Resource
    Electronic Resource
    Plastocyanin is encoded by an uninterrupted nuclear gene in spinach (1986)
    Springer
    Current genetics 11 (1986), S. 171-176 
    Details
    ISSN: 1432-0983
    Keywords: Plastocyanin ; Photosynthesis ; Genomic and cDNA clones ; Sequence analysis ; Transcript ; Spinach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Plastocyanin is a member of photosynthetic electron transport chains that transfers electrons from cytochrome f to the oxidized P700 chlorophyll a pigment of the photosystem I reaction center. We have isolated and characterized cDNA- and genomic clones from spinach (Spinacia oleracea) encoding the complete plastocyanin-precursor polypeptide. The amino acid sequence derived from the nucleotide sequence shows that the precursor consists of 168 amino acid residues including a transit sequence of 69 residues. The precursor polypeptide has a predicted Mr of 16,917, the mature protein of 10,413. The available data indicate that plastocyanin derives probably from a single-copy gene. The coding region contains no intron. The size of the mRNA as determined by S1 nuclease protection experiments is approximately 660 nucleotides, although analysis of different cDNA clones suggests that longer RNA species do exist, approaching the size of the mRNA (850 bases) estimated by Northern blot techniques.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00420603
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  • 4
    Electronic Resource
    Electronic Resource
    Analysis of cDNA clones encoding the entire precursor-polypeptide for ferredoxin: NADP+ oxidoreductase from spinach (1988)
    Springer
    Current genetics 13 (1988), S. 517-522 
    Details
    ISSN: 1432-0983
    Keywords: Photosynthesis ; Ferredoxin-NADP+ oxidoreductase ; cDNA Nucleotide sequence ; Transit peptide ; Spinach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In this paper, we report the structural characterization of several spinach ferredoxin-NADP+ oxidoreductase (FNR) cDNAs ranging in size from 0.9 to 1.5 kilobases. A comparison of the deduced amino acid sequence with the known amino acid sequence determined for the spinach protein establishes that 1.4–1.5 kpb inserts span the full length of the mature protein (314 amino acid residues; Mr = 35,382). These also include an N-terminal 55 amino acid transit peptide as well as maximally 171 and 214 nucleotide 5′ and 3′ untranslated sequences, respectively. Evidence has been obtained that various forms of FNR arise from at least two similar genes. The FNR precursor (369 amino acid residues) has a calculated molecular mass of 41.2 kDa. Comparison of the transit peptide with transit peptides from two other stromal proteins shows little similarity at the level of primary sequence but some common features in secondary structure predictions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02427758
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  • 5
    Electronic Resource
    Electronic Resource
    Nucleotide sequences of cDNA clones encoding the entire precursor polypeptide for subunit VI and of the plastome-encoded gene for subunit VII of the photosystem I reaction center from spinach (1989)
    Springer
    Current genetics 16 (1989), S. 99-108 
    Details
    ISSN: 1432-0983
    Keywords: Photosynthesis ; Photosystem I ; Subunits VI and VII ; Nucleotide sequence ; Spinach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Recombinant phage which encode the entire precursor polypeptide for subunit VI of the photosystem I reaction center have been selected from a lambda gt11 cDNA expression library made from polyadenylated RNA of spinach seedlings. The sequence predicts a precursor polypeptide of 144 amino acids (Mr = 15.3 kDa), a mature protein of 95 residues (Mr = 10.4 kDa) that lacks methionine, histidine and cysteine, and a transit peptide of 49 residues (Mr = 4.9 kDa). The corresponding gene(s) is (are) designated psaH. The gene for subunit VII, psaC, has been located in the small single-copy region of the spinach plastid chromosome using a synthetic oligonucleotide and a heterologous hybridization probe. It is part of a polycistronic transcription unit that is constitutively expressed and processed. Putative processing products include a monocistronic RNA for psaC. The polypeptide chain of 81 (deduced) amino acids is highly conserved and strikingly resembles bacterial-type ferredoxins. It harbours cysteine residues that appear to be involved in the ligation of the two 4Fe4S centres A and B in photosystem I. None of the two subunits appears to be membrane-spanning, and subunit VI, as subunit VII, is located at the reducing (stromal) side of the reaction center. All available information on the major subunits of photosystem I from spinach has been combined into a (revised) topographic model. Evidence that the innermost — plastome-encoded — core of photosystem I represents an old bacterial heritage in present day chloroplasts is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00393402
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  • 6
    Electronic Resource
    Electronic Resource
    Nucleotide sequence of cDNA clones encoding the complete precursor for subunit delta of thylakoid-located ATP synthase from spinach (1988)
    Springer
    Plant molecular biology 10 (1988), S. 323-330 
    Details
    ISSN: 1573-5028
    Keywords: chloroplast ATP synthase ; subunit delta ; cDNA nucleotide sequence ; transit peptide ; spinach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The nucleotide sequence of the entire nuclear-encoded precursor for subunit delta of the ATP synthase from spinach thylakoid membranes was determined by cDNA sequencing. Appropriate recombinant DNAs were selected from pBR322 and lambda gt11 libraries made from polyadenylated RNA of greening spinach seedlings. The mature protein consists of 187 amino acid residues corresponding to a molecular weight of 20468. The precursor protein (257 amino acid residues; M r=27676) is probably processed between a Met-Val bond. The predicted secondary structure of the transit sequence (70 residues; 7.2 kDa) resembles that of the Rieske Fe/S polypeptide, but shows little similarity with those of stromal or luminal proteins. The comparison of the chloroplast delta amino acid sequence with the published delta sequences from respiratory ATP synthases of bacterial and mitochondrial sources and from the thylakoid ATP synthase of the cyanobacterium Synechococcus suggests substantial divergence at the genic level although structural elements appear to be remarkably conserved.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00029882
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  • 7
    Electronic Resource
    Electronic Resource
    Nucleotide sequence of cDNA clones encoding the complete “33 kDa” precursor protein associated with the photosynthetic oxygen-evolving complex from spinach (1987)
    Springer
    Molecular genetics and genomics 207 (1987), S. 288-293 
    Details
    ISSN: 1617-4623
    Keywords: Photosynthetic oxygen evolution ; “33 kDa” protein ; cDNA nucleotide sequence ; Transit peptide ; Spinach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Several cDNA clones encoding the “33 kDa” protein associated with the photosynthetic water oxidation activity of spinach were sequenced. A 1208 bp insert of one of the clones encodes the entire 331 amino acid residues of the precursor protein including 84 amino acids (8.5 kDa) of the amino-terminal transit peptide, 49 bp of the 5′ and 111 bp of the 3′ untranslated segment of the mRNA. The 3′ poly(A) tail starts 19 bp downstream from a putative polyadenylation signal, TATAAA. The hydrophilic mature protein consists of 247 amino acid residues corresponding to an Mr of 26.5 kDa, which is 6.5 kDa smaller than the value determined by SDS-polyacrylamide gel electrophoresis (33–34 kDa), and shows a certain degree of conservation with the putative Mn-complexing active sites of bacterial Mn-dependent superoxide dismutases. The anatomy of the unusually long transit sequence is discussed with regard to current concepts of protein import into and protein routein within the organelle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00331591
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  • 8
    Electronic Resource
    Electronic Resource
    The complete amino-acid sequence of the rieske FeS-precursor protein from spinach chloroplasts deduced from cDNA analysis (1987)
    Springer
    Molecular genetics and genomics 210 (1987), S. 171-177 
    Details
    ISSN: 1617-4623
    Keywords: Photosynthesis ; Rieske iron-sulfur precursor protein ; cDNA nucleotide sequence ; Transit peptide ; Spinach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Summary Several cDNA clones encoding the entire Rieske FeS-precursor protein of the chloroplast cytochrome b 6 f-complex have been isolated by high density plaque immunoscreening of a phage lambda gt11 cDNA expression library, made from poly A+-RNA of spinach seedlings. The identity of the cDNAs has been confirmed by N-terminal amino acid sequencing of the purified protein. The nucleotide sequence indicates a protein of 247 amino acid residues including a putative transit sequence of 68 amino acids corresponding to molecular masses of 26.3 kDa (precursor) and 18.8 kDa (mature protein; 179 amino acid residues). Alignteins of the sequence with sequences from Rieske FeS-proteins of respiratory electron transport chains, two of bacterial and three of mitochondrial origin, shows little sequence homology, but remarkable similarity in secondary structure including a putative N-terminal transmembrane segment of about 25 residues and the peptides CTHLGCV and CPCHGS in the C-terminal region of the protein that are involved in the binding of the Fe2S2-cluster.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00337775
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  • 9
    Electronic Resource
    Electronic Resource
    Interacting cis elements in the plastocyanin promoter from spinach ensure regulated high-level expression (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 602-613 
    Details
    ISSN: 1617-4623
    Keywords: Plastocyanin gene ; Promoter analysis ; cis elements ; Gel retardation ; Spinach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The spinach plastocyanin promoter contains most, if not all, cis elements crucial for its activity downstream of −259 by relative to the transcription start site. The −259/−79 by promoter fragment is capable of conferring glucuronidase (GUS) gene expression on the minimal −90/+3 by 35S RNA promoter of CaMV and −51/+60 by plastocyanin promoter, regardless of its orientation. Using 5′ promoter deletion analysis and site directed mutagenesis we identified three regions, designated PC-1(−195/−188), PC-2 (−179/−164) and PC-3 (−90/−77) for promoter function. An interaction between PC-3 and the upstream elements is required for high levels of expression. All these sequences contain binding sites for protein factors, as shown by gel shift assays. PC-3 includes a binding site with some resemblance to GT-1 box II, but additional nucleotide sequences immediately downstream of this motif, which are conserved among all published plastocyanin promoters, are required as well. The sequence interval −168/−79 by is sufficient to confer light-responsive, organ-specific and chloroplast-dependent GUS gene expression on minimal promoters.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00285284
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