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  • Nucleotide sequence  (3)
  • cDNA nucleotide sequence  (3)
  • 1
    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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  • 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
    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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  • 4
    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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  • 5
    Electronic Resource
    Electronic Resource
    Complete nucleotide sequence of the Oenothera elata plastid chromosome, representing plastome I of the five distinguishable Euoenothera plastomes (2000)
    Springer
    Molecular genetics and genomics 263 (2000), S. 581-585 
    Details
    ISSN: 1617-4623
    Keywords: Key words Euoenothera ; Oenothera elata ; Plastid chromosome ; Nucleotide sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We describe the 159,4443-bp sequence of the plastid chromosome of Oenothera elata (evening primrose). The Oe. elata plastid chromosome represents type I of the five genetically distinguishable basic plastomes found in the subsection Euoenothera. The genus Oenothera provides an ideal system in which to address fundamental questions regarding the functional integration of the compartmentalised genetic system characteristic of the eukaryotic cell. Its highly developed taxonomy and genetics, together with a favourable combination of features in its genetic structure (interspecific fertility, stable heterozygous progeny, biparental transmission of organelles, and the phenomenon of complex heterozygosity), allow facile exchanges of nuclei, plastids and mitochondria, as well as individual chromosome pairs, between species. The resulting hybrids or cybrids are usually viable and fertile, but can display various forms of developmental disturbance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00008686
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  • 6
    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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