Isolation from
            <i>Ochrobactrum anthropi</i>
            of a Novel Class II 5-Enopyruvylshikimate-3-Phosphate Synthase with High Tolerance to Glyphosate

Tian, Yong‐Sheng; Xiong, Ai‐Sheng; Xu, Jing; Wang, Zhao; Gao, Feng; Fu, Xin; Zheng, Jinhai; Peng, Ri‐He; Yao, Quan‐Hong

doi:10.1128/aem.00770-10

Cited by 30 publications

(28 citation statements)

References 24 publications

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“…Numerous amino acid residues that affect EPSPS glyphosate resistance have already been identified (1,8,10,13,15,19,20,24,25,31,35,40,50). Notably, these residues are mostly distributed in two regions according to their 3D structure.…”

Section: Discussionmentioning

confidence: 99%

“…The K m values for PEP, the K i values for glyphosate, and the IC 50 value for glyphosate were measured as described by Tian et al (40).…”

Section: Bacterialmentioning

confidence: 99%

“…Recently, a new gene encoding glyphosate-resistant EPSPS was identified in Ochrobactrum anthropi (40). In the present study, we performed DNA shuffling on the new aroA gene from O. anthropi under selective pressure caused by high glyphosate concentrations.…”

mentioning

confidence: 96%

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Improvement of Glyphosate Resistance through Concurrent Mutations in Three Amino Acids of the Ochrobactrum 5-Enopyruvylshikimate-3-Phosphate Synthase

Tian

Xiong

et al. 2011

Appl Environ Microbiol

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A mutant of 5-enopyruvylshikimate-3-phosphate synthase from Ochrobactrum anthropi was identified after four rounds of DNA shuffling and screening. Its ability to restore the growth of the mutant ER2799 cell on an M9 minimal medium containing 300 mM glyphosate led to its identification. The mutant had mutations in seven amino acids: E145G, N163H, N267S, P318R, M377V, M425T, and P438L. Among these mutations, N267S, P318R, and M425T have never been previously reported as important residues for glyphosate resistance. However, in the present study they were found by site-directed mutagenesis to collectively contribute to the improvement of glyphosate tolerance. Kinetic analyses of these three mutants demonstrated that the effectiveness of these three individual amino acid alterations on glyphosate tolerance was in the order P318R > M425T > N267S. The results of the kinetic analyses combined with a three-dimensional structure modeling of the location of P318R and M425T demonstrate that the lower hemisphere's upper surface is possibly another important region for glyphosate resistance. Furthermore, the transgenic Arabidopsis was obtained to confirm the potential of the mutant in developing glyphosate-resistant crops.

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Section: Discussionmentioning

confidence: 99%

“…The K m values for PEP, the K i values for glyphosate, and the IC 50 value for glyphosate were measured as described by Tian et al (40).…”

Section: Bacterialmentioning

confidence: 99%

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Improvement of Glyphosate Resistance through Concurrent Mutations in Three Amino Acids of the Ochrobactrum 5-Enopyruvylshikimate-3-Phosphate Synthase

Tian

Xiong

et al. 2011

Appl Environ Microbiol

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“…The K m values for PEP, the K i values for glyphosate, and the IC 50 value for glyphosate were determined as described by Tian et al (2010).…”

Section: Epsp Synthase Activitymentioning

confidence: 99%

Multiple mechanism confers natural tolerance of three lilyturf species to glyphosate

Mao

Xie

Chen

et al. 2015

Planta

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A combination of unique EPSPS structure and increased gene copy number and expression contribute to natural glyphosate tolerance in three lilyturf species. A few plants are naturally tolerant to glyphosate, the most widely used non-selective herbicide worldwide. Here, the basis for natural tolerance to glyphosate in three lilyturf species, Ophiopogon japonicus (OJ), Liriope spicata (LS), and Liriope platyphylla (LP), is characterized. These species tolerate glyphosate at about five times the commercially recommended field dose. They share three unique amino acids in their 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) that affect glyphosate binding. These correspond to Asp71Met, Ala112Ile, and Val201Met amino acid variations compared to 231 other published plant EPSPS amino acid sequences. There was also a common deletion at 91 of a highly conserved glutamic acid. Glyphosate-treated lilyturf plants accumulated little shikimic acid but had significantly higher levels of EPSPS mRNA than initially expressed in the control. The IC50 of LsEPSPS was 14.0 µM compared to the 5.1 µM of Arabidopsis thaliana. The higher K m and K i values of LsEPSPS kinetics showed that LsEPSPS had lower substrate binding affinity to glyphosate. Overexpression of LsEPSPS in the recombinant E. coli BL21 (DE3) strain enhanced its tolerance to glyphosate. Both OJ and LS had two copies of the EPSPS gene, while LP had three copies. Therefore, a combination of unique EPSPS structure and increased gene copy number and expression contribute to natural glyphosate tolerance in the three lilyturf species.

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“…Recently, the possible use of class II EPSPS found in Ochrobactrum anthropi has also been considered. [9][10][11][12][13]. At present, after almost 20 years of their presence in agronomy, transgenic varieties constitute the essential profile of continent-wide cultivation.…”

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confidence: 99%

Glyphosate-based phospho-organic herbicides – an outline of action, metabolism and the selected effects on humans and other organisms

Baran¹,

Cibiński²

2014

apgr

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Glyphosate (GP) is an active substance of the most common group of herbicides, applied to large cultivation areas as well as small allotments, home and industrial greeneries, those along traffic routes and around public areas. GP is highly valued for its lack of direct risks to humans and animals or no tendency to bioaccumulate in trophic networks. Over the past four decades of its use, GP was found to be extremely effective. However, controversies over its applications have been growing; therefore, it is increasingly implied that its effects on the environment, living organisms and people residing in it should be verified.

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Isolation from Ochrobactrum anthropi of a Novel Class II 5-Enopyruvylshikimate-3-Phosphate Synthase with High Tolerance to Glyphosate

Cited by 30 publications

References 24 publications

Improvement of Glyphosate Resistance through Concurrent Mutations in Three Amino Acids of the Ochrobactrum 5-Enopyruvylshikimate-3-Phosphate Synthase

Improvement of Glyphosate Resistance through Concurrent Mutations in Three Amino Acids of the Ochrobactrum 5-Enopyruvylshikimate-3-Phosphate Synthase

Multiple mechanism confers natural tolerance of three lilyturf species to glyphosate

Glyphosate-based phospho-organic herbicides – an outline of action, metabolism and the selected effects on humans and other organisms

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