Mutations Resistant to Photosystem II Herbicides

Hirschberg, Joseph; Yehuda, Adi Ben; Pecker, Iris; Ohad, Nir

doi:10.1007/978-1-4615-7598-6_33

Cited by 32 publications

(20 citation statements)

References 48 publications

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“…Much information on the modification of D1 protein in mutants resistant to DCMU and/or atrazine is available in the literature [1][2][3][4][5][6][7][8][9] but nothing concerning phenol-type herbicide-resistant mutants has appeared. These herbicides exhibit several inhibitory effects, including one on the PS II donor side [10,11].…”

Section: Introductionmentioning

confidence: 99%

Mutation in phenol‐type herbicide resistance maps within thepsbA gene inSynechocystis6714

et al. 1989

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A Synechocystis 6714 mutant resistant to the phenol-type herbicide ioxynil was isolated and characterized. Sensitivity to DCMU and atrazine was measured in whole cells and isolated thylakoids. The mutant presents the same sensitivity to atrazine as the wild type and a slightly increased sensitivity to DCMU. A point mutation has been found at codon 266 in the psbAI coding locus (AAC to ACC) resulting in an amino acid change from asparagine to threonine in the D 1 protein.

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Section: Introductionmentioning

confidence: 99%

Mutation in phenol‐type herbicide resistance maps within thepsbA gene inSynechocystis6714

et al. 1989

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“…Amino acids in these positions in D1 of both cyanobacteria and higher plants are known to contribute to the binding of various herbicides [8,16]. A third mutation at position 255 (Tyr5) was subsequently designed and genetically engineered in the same organism so that the wild type and the three mutants would give rise to a thermodynamic cycle that consists of two parallel and identical substitutions: Phe 255 , Tyr 255; Ser 264 ~ Ala 264.…”

Section: Resultsmentioning

confidence: 99%

“…Competition between the herbicides and QB for the same binding site has been demonstrated [5,6]. Different amino acid substitutions in the D1 protein have been previously found to reduce herbicide binding, thereby conferring herbicide-resistance [7,8]. Using site-directed mutagenesis it is possible to replace any amino acid in a protein.…”

Section: Introductionmentioning

confidence: 99%

Predicted effects on herbicide binding of amino acid substitutions in the D1 protein of photosystem II

1989

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The effects of an amino acid substitution in the DI protein of photosystem lI on its binding to different herbicides are here successfully predicted. This is done by assuming additivity in the contributions to the binding energy of the amino acids at positions 255 and 264 of this protein which are part of the herbicide binding niche. Additivity in DI proteinherbicide interactions is demonstrated, thus indicating an apparent lack of interactions between the amino acids at these two positions.

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“…It has been reported that resistance to DCMU is often acquired by an alteration of the herbicidebinding site (D1 protein) on the thylakoid membranes, which results in a reduced affinity of the herbicide with the binding site (Galloway & Mets, 1984;Erickson et al, 1989;Galloway & Mets, 1989). DCMU-resistant mutants of higher plants and green algae were shown to involve single amino-acid substitutions in the D1 protein (Hirschberg & McIntosh, 1983;Hirschberg et al, 1987;Erickson et al, 1989;Mengistu et al, 2000Mengistu et al, , 2005. Such mutants usually present additional pleiotropic effects, such as an increased sensitivity to strong illumination (Sundby et al, 1993;Alfonso et al, 1996), tolerance to irradiance (Singh & Singh, 1997), tolerance to heat stress (Alfonso et al, 2001) and tolerance to salt stress (Singh & Kshatriya, 2002).…”

Section: Introductionmentioning

confidence: 99%

DCMU-resistance mutation confers resistance to high salt stress in the red microalgaPorphyridiumsp. (Rhodophyta)

Manandhar-Shrestha

Arad

Vonshak

2009

European Journal of Phycology

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The response of photosynthesis to salinity stress in wild-type and DCMU-resistant (strain DC-2) Porphyridium sp. was investigated. Both wild-type and DC-2 were able to acclimate and establish a new steady state of growth when exposed to salt stress, but growth rate of the DC-2 mutant strain was 1.25-fold higher than growth rate of wild-type cells. Following establishment of a new steady state under the salt stress conditions, the maximal irradiance-saturated photosynthetic capacity (P max ), light saturation (I k ) and the photosynthetic efficiency () were 1.5-, 1.8-and 1.1-fold, respectively, higher in the DC-2 mutant cells than wild-type. Furthermore, salt-stressed DC-2 mutant cells exhibited 1.6-fold higher maximal efficiency of PS II (Fv/Fm) after 200 min exposure and 3-fold higher level of D1 protein after 24 h exposure to salt than wild-type cells. Exposing the salt-stressed cells to high photon flux density (3000 mmol m -2 s -1 ) for 1 h resulted in a higher resistance of mutant cells than wild-type to light stress, as reflected in 1.3-fold decline in the Fv/Fm. This finding corresponds well with the levels of the D1 protein measured in the cells. These observations indicate that the D1 protein of the PS II apparatus in the DC-2 mutant was more resistant to stress. However, under non-stressed (light and salt) conditions, no differences were observed between wild-type and the DC-2 mutant cells for all the parameters studied. The DC-2 mutant responded better than wild-type to environmental stresses, namely salinity and light due to the modification induced in PS II.

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Mutations Resistant to Photosystem II Herbicides

Cited by 32 publications

References 48 publications

Mutation in phenol‐type herbicide resistance maps within thepsbA gene inSynechocystis6714

Mutation in phenol‐type herbicide resistance maps within thepsbA gene inSynechocystis6714

Predicted effects on herbicide binding of amino acid substitutions in the D1 protein of photosystem II

DCMU-resistance mutation confers resistance to high salt stress in the red microalgaPorphyridiumsp. (Rhodophyta)

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