Computational insights into evolutionary and functional biology of plant cell wall degrading pectate lyases from plant parasitic nematodes of the order Tylenchida

文献类型： 外文期刊

第一作者： Zahoor, Adil

作者： Zahoor, Adil;Niaz, Zeenat;Ali, Muhammad Amjad;Seo, Hyojin;Jabran, Muhammad;Azeem, Farrukh;Joyia, Faiz Ahmad;Nawaz, Muhammad Amjad;Zahoor, Adil;Yang, Seung Hwan

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关键词： pectate lyases; Tylenchida; in silico characterization; nomenclature; evolutionary analysis; molecular docking

期刊名称：PAKISTAN JOURNAL OF AGRICULTURAL SCIENCES （ 影响因子：0.8； 五年影响因子：0.8 ）

ISSN： 0552-9034

年卷期： 2023 年 60 卷 1 期

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收录情况： SCI

摘要： Plant parasitic nematodes (PPNs) develop sophisticated feeding sites in plant roots called nematode feeding sites (NFSs). The development of NFSs depends on the degradative role of particular cell wall degrading enzymes, namely, cellulases, xylanases, arabinases, and pectate lyases (Pels). The esophageal glands of PPNs secrete the Pels into the host cell's cytoplasm to invade and macerate the host root tissues. Considerable research has been conducted exploring the Pels of pathogenic bacteria and fungi; however, a detailed Pel characterization has not yet been done for PPNs. This study primarily aims to characterize and investigate Pels' evolutionary and functional dynamics in PPNs of the order Tylenchida. Consequently, Tylenchida Pels were found to be evolutionarily derived into two major clades. Clade-1 lineage meets with the Pels of sub-family_3, whereas the lineage of Clade-2 meets with subfamily_2 of polysaccharide lyases family 3. Structurally, Clade-1 Pels exhibit eight turns of 0-strands, whereas Clade-2 comprises seven turns of 0-strands. Molecular docking of Pels with the substrate molecule alpha-D-galacturonic acid revealed a mechanistically appealing role of Turn 1, 0-strand, and Turn 3 in catalytic activity, ultimately enhancing the understanding of the degradation mechanism of pectin through Pels.

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