| | 2 | Author
| I. Perewoska, C. Vernotte, M. Picaud, C. Astier | Requires 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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| default:Reihe_C/47/ZNC-1992-47c-0580.pdf | | | | Identifier
| ZNC-1992-47c-0580 | | | | Volume
| 47 | |
| 3 | Author
| Dirk Naber, Udo Johanningmeier, JackJ S Van Rensen, D. N., J.J S V R | Requires 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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| default:Reihe_C/45/ZNC-1990-45c-0418.pdf | | | | Identifier
| ZNC-1990-45c-0418 | | | | Volume
| 45 | |
| 4 | Author
| MichaelD. Partis, A.F R, R.Udolf Grimm | Requires 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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| default:Reihe_C/45/ZNC-1990-45c-0987.pdf | | | | Identifier
| ZNC-1990-45c-0987 | | | | Volume
| 45 | |
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