Phototrophic microorganisms in the symbiotic communities of Baikal sponges: Diversity of psbA gene (encoding D1 protein of photosystem II) sequences

A new Synechocystis 6714 mutant, loxIIA, resistant to the phenol-type herbicide ioxynil was isolated and characterized. The mutation found in the psbA gene (encoding the D1 photosystem II protein) is at the same codon 266 as for the first ioxynil-resistant mutant IoxIA previously selected [G. Ajlani. I. Meyer, C. Vernotte. and C. Astier, FEBS Lett. 246, 207-210 (1989)]. In IoxIIA, the change of Asn 266 to Asp gives a 3 × resistance, whereas in IoxIA, the change of the same amino acid to Thr gives a 10 × resistance. The effect of these different amino acid substitutions on the ioxynil resistance phenotype has allowed us to construct molecular models and calculate the hydrogen-bonding energies between the hydroxyl group of ioxynil and the respective amino acids at position 266.

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Heteroplasmy and atrazine resistance in Chenopodium album and Senecio vulgaris

Zeitschrift für Naturforschung C ◽

10.1515/znc-2015-0163 ◽

2016 ◽

Vol 71 (7-8) ◽

pp. 267-272

Author(s):

Michaela Bühler ◽

Arno Bogenrieder ◽

Heinrich Sandermann ◽

Dieter Ernst

Keyword(s):

Photosystem Ii ◽

Chenopodium Album ◽

D1 Protein ◽

Base Substitution ◽

Individual Plant ◽

Chloroplast Gene ◽

Gene Encoding ◽

Senecio Vulgaris ◽

Different Types ◽

Binding Sequence

Abstract Atrazine-resistant weeds are well known, and the resistance is primarily caused by a point mutation in the psbA chloroplast gene encoding the photosystem II D1 protein. Heteroplasmy, the presence of different types of chloroplasts in an individual plant, is also very common. Thus, atrazine-resistant weeds may also partly possess the atrazine-binding sequence and vice versa. The region of the psbA gene containing the mutation was sequenced from atrazine-resistant and atrazine-sensitive Chenopodium album and Senecio vulgaris plants. In atrazine-sensitive C. album plants, the expected AGT triplet was found. The atrazine-resistant plants contained the expected base substitution (AGT to GGT); however, in addition the AGT triplet was found. The atrazine-resistant S. vulgaris plants contained the expected GGT sequence, whereas the atrazine-sensitive plants contained both the AGT and GGT sequences. This clearly indicates that in addition to Gly264 also Ser264 is present in atrazine-resistant plants, and vice versa in atrazine-sensitive plants, indicating heteroplasmy in these weeds.

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The emergence of a atrazine resistant black nightshade (Solanum nigrum L.) biotype and molecular basis of the resistance

Plant Protection Science ◽

10.17221/1470-pps ◽

2010 ◽

Vol 40 (No. 3) ◽

pp. 94-100 ◽

Cited By ~ 1

Author(s):

J. Salava ◽

D. Chodová ◽

K. Nováková

Keyword(s):

Chlorophyll Fluorescence ◽

Photosystem Ii ◽

Rapid Detection ◽

Molecular Basis ◽

Restriction Analysis ◽

D1 Protein ◽

Solanum Nigrum ◽

Gene Encoding ◽

Black Nightshade ◽

Pcr Products

Seeds from atrazine resistant plants of black nightshade (Solanum nigrum L.) were collected at the railway station Prague-Vršovice, seeds from susceptible plants in Vyšehořovice (Prague East district). Tests on emergence showed that in both resistant and susceptible biotypes it was highest at a seeding depth of 1 mm, and that at the same seeding depth there were statistically significant differences in emergence between the resistant and susceptible biotypes. The resistance or susceptibility to atrazine was tested by both a chlorophyll fluorescence assay and spraying with atrazine. A region of the gene encoding D1 protein of photosystem II was sequenced and compared between the resistant and susceptible biotypes. Resistance to atrazine in the S. nigrum biotype from Vršovice was conferred by a glycine for serine substitution at residue 264 of the D1 protein. In the plants of the biotypes there was excellent correspondence between the presence of the mutation and herbicide resistance. The assay based on restriction analysis of PCR products can be used for rapid detection of the mutation in populations of black nightshade.

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Inhibition of Photosystem II by Ioxynil in Wild Type and Resistant Mutant of Synechocystis 6714

Zeitschrift für Naturforschung C ◽

10.1515/znc-1989-11-1218 ◽

1989 ◽

Vol 44 (11-12) ◽

pp. 979-984 ◽

Cited By ~ 6

Author(s):

G. Ajlani ◽

I. Meyer ◽

C. Astier ◽

C. Vernotte

Keyword(s):

Electron Transfer ◽

Photosystem Ii ◽

Resistant Mutant ◽

Psba Gene ◽

Wild Type ◽

Donor Side ◽

Gene Encoding ◽

Acceptor Side

Abstract A Synechocystis 6714 mutant resistant to the phenol-type herbicide ioxynil was isolated and characterized. Ioxynil was shown to inhibit both the donor and the acceptor sides of photosystem II, but at different concentrations. The mutation found in the psbA gene (encoding the D, protein) at codon 266 (asparagine to threonine) [G. Ajlani, I. Meyer, C. Vernotte, and C. Astier, FEBS Lett. 246, 207-210 (1989)] gives a ten-fold resistance of the acceptor side to ioxynil without any modification of the sensitivity of the donor side. Electron transfer between the primary and the secondary acceptor of photosystem II was identical in the mutant and the wild type. The mutant remains sensitive to atrazine and is even more sensitive to DCMU than the wild type.

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A Rapid Method for Partial mRNA and DNA Sequence Analysis of the Photosystem II psbA Gene

Zeitschrift für Naturforschung C ◽

10.1515/znc-1990-0518 ◽

1990 ◽

Vol 45 (5) ◽

pp. 418-422 ◽

Cited By ~ 7

Author(s):

Dirk Naber ◽

Udo Johanningmeier ◽

Jack J. S. van Rensen

Keyword(s):

Sequence Analysis ◽

Photosystem Ii ◽

Chenopodium Album ◽

D1 Protein ◽

Single Amino Acid ◽

Amino Acid Substitutions ◽

Psba Gene ◽

Model Species ◽

Resistant Plant ◽

Herbicide Resistant

Abstract Single amino acid substitutions in the D1 protein of photosystem II may cause resistance to various herbicides. In all organisms studied these substitutions are located in or between helices IV and V of the protein. The increasing number of herbicide-resistant organisms necessitates 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 D1. These procedures involve the isolation and amplification of DNA and R A and subsequent sequencing reactions without the need to clone the psbA gene. A triazine-resistant 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 D1 protein, is found in the resistant plant.

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