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'Sequence Analysis' in keywords Facet   section ZfN Section C  [X]
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1992 (1)
1990 (3)
1Author    G. Ewald, C. Wiessner, H. MichelRequires cookie*
 Title    Sequence Analysis of Four Atrazine-Resistant Mutants from Rhodopseudomonas viridis  
 Abstract    Four atrazine-resistant mutants from the purple bacterium Rhodopseudom onas viridis were isolated. Sequence analysis revealed three different mutant strains carrying mutations in the herbicide-binding pocket: i) M AV 2: L 212-G lu —* Lys, ii) M AV 3: L216-Phe —» Ser and iii) M AV 4 = MAV 5: L217-Arg His, L220-Val Leu. Except M AV 3 all Rps. viridis mutants are different from those selected by their resistance towards the closely related triazine terbutryn. 
  Reference    Z. Naturforsch. 45c, 459 (1990); received December 9 1989 
  Published    1990 
  Keywords    Herbicide-Resistant Mutants, Atrazine, Photosynthetic Reaction Center, Sequence Analysis 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0459.pdf 
 Identifier    ZNC-1990-45c-0459 
 Volume    45 
2Author    I. Perewoska, C. Vernotte, M. Picaud, C. AstierRequires cookie*
 Title    Mutations in the Subunit of Photosystem II and Resistance to the Phenol Type Herbicide Ioxynil in Synechocystis PCC 6714 and 6803  
 Abstract    Several herbicides block the photosystem II electron transfer because they compete with QB, the second stable electron acceptor o f photosystem II for binding to the D, subunit. We have previously isolated a mutant o f Synechocystis 6714 in which Asn is replaced by Thr at position 266 o f D, (G. Ajlani, I. Meyer, C. Vernotte, and Astier, FEBS Lett. 246, 2 0 7 -2 1 0 (1989)) and presenting resistance to ioxynil but not to D C M U . In this report we present selection, from this mutant, o f a double mutant with an additional substitution at position 264 (Ser by Ala). The sensitivity o f this mutant toward several herbicides is given and compared to those o f the mutants having only one substitution at 266 and one substitution at 264. It was also compared to a mutant o f Chlamydomonas having the same substitutions. This allows us to discuss the interaction o f various herbicides with the D , protein and to compare the herbicide binding niches o f Chlamydomonas and Synechocystis. 
  Reference    Z. Naturforsch. 47c, 580—5 (1992); received March 13 1992 
  Published    1992 
  Keywords    Cyanobacteria, Chlamydomonas, Herbicide-Resistant M utants, Photosynthesis, Sequence Analysis 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0580.pdf 
 Identifier    ZNC-1992-47c-0580 
 Volume    47 
3Author    Dirk Naber, Udo Johanningmeier, JackJ S Van Rensen, D. N., J.J S V RRequires cookie*
 Title    A Rapid Method for Partial mRNA and DNA Sequence Analysis of the Photosystem II psbA Gene  
 Abstract    Single amino acid substitutions in the D 1 protein of photosystem II may cause resistance to various herbicides. In all organisms studied these substitutions are located in or between hel­ ices IV and V of the protein. The increasing number of herbicide-resistant organisms necessi­ tates development of a rapid methodology to characterize deviations from the wildtype se­ quence. Here, two procedures are described to identify mutations in the psbA gene, which is coding for D 1. These procedures involve the isolation and amplification of D N A and RN A and subsequent sequencing reactions without the need to clone the psbA gene. A triazine-re-sistant and a -susceptible biotype of Chenopodium album were used as model species. An A to G transition, giving rise to a serine to glycine mutation at position 264 in the D 1 protein, is found in the resistant plant. 
  Reference    Z. Naturforsch. 45c, 418—422 (1990); received November 3 1989 
  Published    1990 
  Keywords    Triazine Resistance, Sequence Analysis, Polymerase Chain Reaction, Chenopodium album 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0418.pdf 
 Identifier    ZNC-1990-45c-0418 
 Volume    45 
4Author    MichaelD. Partis, A.F R, R.Udolf GrimmRequires cookie*
 Title    Computer Analysis of Phytochrome Sequences from Five Species: Implications for the Mechanism of Action  
 Abstract    The amino acid sequences o f phytochrom e from A vena sativa, O ryza sativa, Curcurbita pepo, Pisum sativum and Arabidopsis thaliana have been analyzed with a variety o f computer programs, with a view to identifying areas o f the protein which contribute to the properties o f this photoreceptor. A region at the C-terminus has been shown to be amphiphilic, and by ana­ logy with surface-seeking peptides, may be responsible for interaction o f phytochrom e with lipid bilayers. Possible targeting sequences in phytochrom es have been identified, including a series o f four basic residues which correspond to those responsible for transport o f nuclear-located proteins. Sites capable o f post-translational m odification have been found in m onocot sequences, but not in dicot sequences. Areas o f the phytochrom e molecule which are exposed on the surface o f the portein, and which are therefore capable o f interaction with other cellular macromolecules, have been identified. A nalogies with other biliproteins have been used to de­ fine minimum chromophore-protein interactions. Possible enzymic activities associated with phytochromes have been discussed with respect to local amino acid sequence similarity with enzymes. 
  Reference    Z. Naturforsch. 45c, 987—9 (1990); received April 12 1990 
  Published    1990 
  Keywords    Phytochrome, Sequence Analysis, Amphiphilic Peptides, M embrane Interaction, Targeting Sequences 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0987.pdf 
 Identifier    ZNC-1990-45c-0987 
 Volume    45