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'Cyanobacteria' in keywords Facet   Publication Year 1992  [X]
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1992[X]
1Author    H.E A Schenk, M. G. Bayer, T. L. Maier, A. Lüttke, U.B G Ebhart, S. StevanovicRequires cookie*
 Title    Ferredoxin-NADP+ Oxidoreductase of C. paradoxa Nucleus Encoded, but Cyanobacterial Gene Transfer from Symbiont to Host, an Evolutionary Mechanism Originating New Species  
 Abstract    The nucleus encoded cyanoplast ("cyanellar") ferredoxin-N A D P+ -oxidoreductase (F N R) o f Cyanophora paradoxa, characterized by an N-terminal amino acid sequence, is compared with hom ologous sequences o f other photoautotrophic organisms. The high degree o f similari­ ty to the cyanobacterial sequences indicates a cyanobacterial origin. This could be a first direct demonstration o f an intertaxonic combination; a gene transfer from an original endocytobiont (cyanobacterium) to the nucleus o f its host, one o f the most important demands o f the Endo-symbiosis Theory, an evolutionary mechanism leading to the origin o f a new species. 
  Reference    Z. Naturforsch. 47c, 387—3 (1992); received December 4 1991/February 10 1992 
  Published    1992 
  Keywords    C yanophoraparadoxa, G laucocystophyta, Cyanobacteria, Cyanelles, Cyanoplasts 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0387.pdf 
 Identifier    ZNC-1992-47c-0387 
 Volume    47 
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    DirkH. Engels, Anke Engels, ElfriedeK. PistoriusRequires cookie*
 Title    Isolation and Partial Characterization of an l -Amino Acid Oxidase and of Photosystem II Complexes from the Cyanobacterium Synechococcus PCC 7942  
 Abstract    An L-amino acid oxidase with high specifity for basic L-amino acids was isolated from the cyanobacterium Synechococcus PCC 7942, and the enzyme was partially characterized. This enzyme was compared to the previously described L-amino acid oxidase from Synechococcus 
  Reference    Z. Naturforsch. 47c, 859 (1992); received October 4 1992 
  Published    1992 
  Keywords    Cyanobacteria, Synechococcus PCC 7942, Photosystem II, L-Amino Acid Oxidase, Water Oxi­ dizing Enzyme 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0859.pdf 
 Identifier    ZNC-1992-47c-0859 
 Volume    47 
4Author    Klaus-Peter Michel, ElfriedeK. Pistorius, E. Gau, G. Wälzlein, S. Gärtner, M. Kuhlmann, E. K. PistoriusRequires cookie*
 Title    Isolation of a Photosystem II Associated 36 kDa Polypeptide and an Iron-Stress 34 kDa Polypeptide from Thylakoid Membranes of the Cyanobacterium Synechococcus PCC 6301 Grown under Mild Iron Deficiency  
 Abstract    A 36 kDa polypeptide which previously was shown to be present in purified photosystem II complexes from Synechococcus PCC 6301 and which crossreacts with the antiserum raised against the soluble L-amino acid oxidase o f 50 kD a from Synechococcus PCC 6301 (A. was isolated from thylakoid membranes o f the same cyanobacterium grown under mild iron deficiency. This peptide is present in about equal am ounts in thylakoid membranes o f Syne­ chococcus PCC 6301 grown under regular or iron deficient conditions. The antiserum raised against this thylakoid membrane bound 36 kD a peptide crossreacts with the soluble L-amino acid oxidase o f 50 kDa. These results further support our conclusion that the thylakoid mem­ brane bound 36 kD a polypeptide is a modified form o f the soluble 50 kD a L-amino acid oxi­ dase. In addition, a 34 kD a polypeptide was isolated from iron stressed thylakoid membranes, and an antiserum was also raised against this protein. Im m unoblot experiments with this an­ tiserum show that the 34 kD a peptide is present in elevated amounts in thylakoid membranes from Synechococcus cells grown under iron deficiency and that it is alm ost absent in thylakoid membranes from cells grown under regular conditions. 
  Reference    Z. Naturforsch. 47c, 867—8 (1992); received August 4/O ctober 8 1992 
  Published    1992 
  Keywords    Cyanobacteria, Synechococcus PCC 6301, Photosystem II, L-Amino Acid Oxidase, Iron Stress 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0867.pdf 
 Identifier    ZNC-1992-47c-0867 
 Volume    47