MurA- catalyzed synthesis of 5-enolpyruvylshikimate-3-phosphate confers tolerance in

• 成果类型: Article
• 署名作者: Caygill, Samuel; Koecher, Thomas; Dolan, Liam
• 署名单位: Austrian Academy of Sciences; Vienna Biocenter (VBC); Gregor Mendel Institute of Molecular Plant Biology (GMI); University of Oxford; Vienna Biocenter (VBC)
• 刊物名称: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
• ISSN/ISSBN: 0027-10185
• DOI: 10.1073/pnas.2412997121
• 发表日期: 2024-11-19
• 关键词: udp-n-acetylglucosamine; enolpyruvyl transferase mura; epsps gene amplification; alanine-adding enzyme; 3-phosphate synthase; glyphosate resistance; molecular-basis; plant; peptidoglycan; ACID

摘要

Glyphosate is a broad- spectrum herbicide that kills most vascular plant weeds but is ineffective against many bryophytes. Glyphosate competitively inhibits the enolpyruvyl transferase enzyme 5- enolpyruvylshikimate-3- phosphate synthase (EPSPS). EPSPS catalyzes the production of 5- enolpyruvylshikimate-3- phosphate (EPSP)-an intermediate in the shikimate pathway-from shikimate-3- phosphate (S3P) and phosphoenolpyruvate (PEP) substrates. Here, we show that Marchantia polymorpha mutants with loss- of- function mutations in a closely related enolpyruvyl transferase, Mp MurA, were more sensitive to glyphosate than wild- type controls. Overexpression of Mp MurA in M. polymorpha increased glyphosate tolerance, and heterologous expression of the M. polymorpha MurA enzyme in Arabidopsis thaliana conferred glyphosate resistance. Furthermore, we demonstrate that MpMurA catalyzes the production of EPSP from S3P and PEP substrates. These data demonstrate that MpMurA contributes to glyphosate tolerance in M. polymorpha. We speculate that the existence of two independent mechanisms for EPSP synthesis-one canonical and EPSPS- dependent, and the other MurA- dependent-may account for glyphosate tolerance in bryophytes. Alternatively, MurA in bryophytes may bind glyphosate, thereby leaving more unbound EPSPS enzymes available, allowing aromatic amino acid biosynthesis to continue.