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  • cDNA nucleotide sequence  (3)
  • Key wordsOenothera  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Plant regeneration from leaf protoplasts of evening primrose (Oenothera hookeri) (1998)
    Springer
    Plant cell reports 17 (1998), S. 601-604 
    Details
    ISSN: 1432-203X
    Keywords: Key wordsOenothera ; Leaf protoplasts ; Thin-alginate-layer technique ; Plant regeneration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A protocol is presented for regenerating plants from leaf protoplasts of Oenothera. The method uses (1) embedding of isolated protoplasts at high cell densities in thin alginate layers, (2) initial culture in B5 medium containing 3 mg l–1 α-naphthaleneacetic acid (NAA) and 1 mg l-1 6-benzylaminopurine (BAP), (3) reduction of the osmotic pressure of the culture medium at early stages of culture and (4) plating of microcolonies recovered from the alginate onto solid B5 medium with 3 mg l–1 NAA and 1 mg l–1 BAP. The shortest time required from protoplast isolation to the appearance of shoot initials was 7 weeks. The efficiency of the procedure for protoplast to cell line formation is high (about 80%).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002990050450
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  • 2
    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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  • 3
    Electronic Resource
    Electronic Resource
    Tissue culture of wild-type, interspecific genome/plastome hybrids and plastome mutants of evening primrose (Oenothera): controlled morphogenesis and transformation (1998)
    Springer
    Plant cell reports 17 (1998), S. 605-611 
    Details
    ISSN: 1432-203X
    Keywords: Key wordsOenothera ; In vitro culture ; Regeneration ; Transformation ; Agrobacterium tumefaciens
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A favourable combination of genetic features in the genus Oenothera offers access to fundamental biological aspects that are not readily approached with other materials. We have developed protocols for cell and tissue culture as well as for transformation, in order to establish the basis for a comprehensive cell and molecular biology of Euoenothera species, their genome/plastome hybrids and plastome mutants. Regeneration of plants from excised seedling parts (roots, hypocotyl, cotyledons, shoot tips) and leaf explants was optimal on NT medium containing 1 mg ⋅ l–1 6-benzylaminopurine and 3 mg ⋅ l–1 α-naphtalene acetic acid. This medium also proved to be efficient in the propagation of various wild-type genotypes, interspecific hybrids and plastome mutants. Using Ti-based approaches we also succeeded in generating transgenic Oenothera plants with relatively high efficiency.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002990050451
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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
    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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