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Functional and Structural Analysis of a Novel Acyltransferase from Pathogenic Phytophthora melonis

文献类型： 外文期刊

作者： Ahmad, Aqeel 1 ; Akram, Waheed 1 ; Bashir, Zoobia 2 ; Shahzadi, Iqra 3 ; Wang, Rui 1 ; Abbas, Hafiz Muhammad Khalid 1 ;

作者机构： 1.Guangdong Acad Agr Sci, Vegetable Res Inst, Guangdong Key Lab New Technol Res Vegetables, Guangzhou 510640, Peoples R China

2.Nanjing Univ, Dept Phys, Natl Lab Solid State Microstruct, Nanjing 210093, Jiangsu, Peoples R China

3.Wuhan Univ, Sch Resource & Environm Sci, Wuhan 430072, Hubei, Peoples R China

4.Univ Austral Chile, Fac Ciencias, Inst Farm, Valdivia 5090000, Chile

期刊名称：ACS OMEGA （ 影响因子：3.512； 五年影响因子：3.613 ）

ISSN： 2470-1343

年卷期： 2021 年 6 卷 3 期

页码：

收录情况： SCI

摘要： This investigation characterizes an acyltransferase enzyme responsible for the pathogenicity of Phytophthora melonis. The protein was characterized in vitro for its physicochemical properties. The biochemical characterization, including thermal and pH stability, revealed the 35 degrees C temperature and 7.0 pH as the optimum conditions for the enzyme. Applying the Tween-80 solution enhanced the activity up to 124.9%. Comprehensive structural annotation revealed two domains, A (ranging from residues 260 to 620) and B (ranging from 141 to 219). Domain A had transglutaminase (T-Gase) elicitor properties, while B possessed antifreeze features. Rigorous sequence characterization of the acyltransferase tagged it as a low-temperature-resistant protein. Further, the taxonomic distribution analysis of the protein highlighted three genera in Oomycetes, i.e., Pythium, Phytophthora, and Plasmopara, bearing this protein. However, some taxonomic groups other than Oomycetes (i.e., archaea and bacteria) also contained the protein. Functional studies of structurally analogous proteins spanned 10 different taxonomic groups. These revealed TGase elicitors (10%), phytopathogen effector proteins RxLR (4%), transporter family proteins (3%), and endonucleases (1%). Other analogues having one percent of their individual share were HIV tat-specific factor 1, protocadherin fat 4, transcription factor 1, and 3-hydroxyisobutyrate dehydrogenase. Because the plant infection by P. melonis is a complex process regulated by a profusion of extracellular signals secreted by both host plants and the pathogen, this study will be of help in interpreting the cross-talk in the host-pathogen system.

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