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

1990 ◽  
Vol 45 (5) ◽  
pp. 418-422 ◽  
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.

A Herbicide Resistant Euglena Mutant Carrying a Ser to Thr Substitution at Position 265 in the D1 Protein of Photosystem II

1992 ◽  
Vol 47 (3-4) ◽  
pp. 245-248 ◽  
Author(s):  
A. Aiach ◽  
E. Ohmann ◽  
U. Bodner ◽  
U. Johanningmeier
Keyword(s):  
Amino Acids ◽  
Sequence Analysis ◽  
Photosystem Ii ◽  
D1 Protein ◽  
Inhibitory Effect ◽  
Wild Type ◽  
Rna Sequence ◽  
Herbicide Resistant ◽  
Lower Resistance ◽  
Chlamydomonas Mutants

A herbicide resistant Euglena mutant (MSI) has been obtained by adapting wild type cells to increasing concentrations of DCMU (3-(3′,4′-dichlorophenyl)-1,1-dimethylurea). Lower resistance levels towards DCMU and metribuzin were observed in MSI when compared with Euglena or Chlamydomonas mutants with Ser 264 to Ala substitutions. RNA-sequence analysis identified a Ser to Thr change at position 265 (equivalent to position 264 in other organisms), thus making it possible to compare the influence of amino acids Ser, Ala and Thr at identical positions on the inhibitory effect of structurally different herbicides in the same species.

Engineered ectopic expression of the psbA gene encoding the photosystem II D1 protein in Synechocystis sp. PCC6803

2007 ◽  
Vol 92 (3) ◽  
pp. 315-325 ◽  
Author(s):  
Madhavi Kommalapati ◽  
Hong Jin Hwang ◽  
Hong-Liang Wang ◽  
Robert L. Burnap
Keyword(s):  
Photosystem Ii ◽  
Ectopic Expression ◽  
D1 Protein ◽  
Psba Gene ◽  
Gene Encoding ◽  
Synechocystis Sp

A New Ioxynil-Resistant Mutant in Synechocystis PCC 6714: Hypothesis on the Interaction of Ioxynil with the D1 Protein

1990 ◽  
Vol 45 (5) ◽  
pp. 436-440 ◽  
Author(s):  
S. Creuzet ◽  
G. Ajlani ◽  
C. Vernotte ◽  
C. Astier
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
D1 Protein ◽  
Resistant Mutant ◽  
Hydroxyl Group ◽  
Amino Acid Substitutions ◽  
Psba Gene ◽  
Molecular Models ◽  
Gene Encoding ◽  
Synechocystis Pcc 6714

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.

Heteroplasmy and atrazine resistance in Chenopodium album and Senecio vulgaris

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.

Photoinactivation and recovery of photosystem II in Chenopodium album leaves grown at different levels of irradiance and nitrogen availability

2002 ◽  
Vol 29 (7) ◽  
pp. 787 ◽  
Author(s):  
Masaharu C. Kato ◽  
Kouki Hikosaka ◽  
Tadaki Hirose
Keyword(s):  
Photosystem Ii ◽  
Protein Turnover ◽  
Nitrogen Availability ◽  
Photosynthetic Capacity ◽  
Chenopodium Album ◽  
D1 Protein ◽  
High Light ◽  
High Nitrogen ◽  
Low Light ◽  
Low Nitrogen

Involvement of photosynthetic capacity and D1 protein turnover in the susceptibility of photosystem II (PSII) to photoinhibition was investigated in leaves of Chenopodium album L. grown at different combinations of irradiance and nitrogen availability: low light and high nitrogen (LL-HN); high light and low nitrogen (HL-LN); and high light and high nitrogen (HL-HN). To test the importance of photosynthetic capacity in the susceptibility to photoinhibition, we adjusted growth conditions so that HL-HN plants had the highest photosynthetic capacity, while that of LL-HN and HL-LN plants was lower but similar to each other. Photoinhibition refers here to net inactivation of PSII determined by the balance between gross inactivation (photoinactivation) and concurrent recovery of PSII via D1 protein turnover. Leaves were illuminated both in the presence and absence of lincomycin, an inhibitor of chloroplast-encoded protein synthesis. Susceptibility to photoinhibition was much higher in plants grown in low light (LL-HN) than those grown in high light (HL-HN and HL-LN). Susceptibility to photoinhibition was similar in HL-LN and HL-HN plants, suggesting that higher photosynthetic energy consumption alone did not mitigate photoinhibition. Experiments with and without lincomycin showed that high-light-grown plants had a lower rate of photoinactivation and a higher rate of concurrent recovery, and that these rates were not influenced by nitrogen availability. These results indicate that turnover of D1 protein plays a crucial role in photoprotection in high-light-grown plants, irrespective of nitrogen availability. For low-nitrogen-grown plants, higher light energy dissipation by other mechanisms may have compensated for lower energy utilization by photosynthesis.

A serine-to-threonine mutation in linuron-resistantPortulaca oleracea

Weed Science ◽  
1999 ◽  
Vol 47 (4) ◽  
pp. 393-400 ◽  
Author(s):  
Joseph G. Masabni ◽  
Bernard H. Zandstra
Keyword(s):  
Electron Transport ◽  
Sequence Analysis ◽  
Time Course ◽  
Chenopodium Album ◽  
Photochemical Efficiency ◽  
D1 Protein ◽  
Cross Resistance ◽  
Fresh Weight ◽  
Electrode Resistance

We conducted several experiments on linuron-resistant and -susceptiblePortulaca oleraceaand on atrazine-resistant and -susceptibleChenopodium albumto determine their immediate and long-term responses to photosynthesis-inhibiting herbicides. Several photosynthesis-inhibiting herbicides were used, and O2evolution was measured with a Clark-type O2electrode. Resistance ratios (RRs) forP. oleracea, based on O2evolution inhibition, were 8 and > 6 for linuron and diuron, respectively; > 800 for atrazine; and > 20 for terbacil. Linuron-resistantP. oleraceawas negatively cross-resistant to bentazon and pyridate (RR = 0.5 and 0.75, respectively). Time-course measurements of fresh weight, photosynthetic CO2assimilation, and photochemical efficiency indicated that linuron and atrazine inhibited electron transport in susceptible (S)P. oleraceaandC. album, ultimately resulting in death. Measurements of photochemical efficiency and CO2assimilation of linuron-resistantP. oleraceatreated with linuron indicated a transient injury from which plants recovered within 14 d. Recovery of linuron-resistantP. oleraceafrom atrazine injury was more rapid than from linuron injury for all measured variables. Atrazine-resistantC. albumhad no cross-resistance to linuron. Sequence analysis of the D1 protein revealed that linuron-resistantP. oleraceahad a serine-to-threonine substitution at position 264.

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