نویسندگان | Shahnoush Nayeri - Bahram Baghban Kohnehrouz - Asadollah Ahmadikhah - Nasser Mahna |
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نشریه | Plant Biotechnology Journal |
شماره صفحات | 1197-1212 |
شماره مجلد | 220 |
نوع مقاله | Original Research |
تاریخ انتشار | 2022 |
رتبه نشریه | ISI |
نوع نشریه | چاپی |
کشور محل چاپ | ایران |
چکیده مقاله
Cellulose is the most abundant unique biopolymer in nature with widespread applications in bioenergy and high‐value bioproducts. The large transmembrane‐localized cellulose synthase (CESA) complexes (CSCs) play a pivotal role in the biosynthesis and orientation of the para‐crystalline cellulose microfibrils during secondary cell wall (SCW) deposition. However, the hub CESA subunit with high potential homo/heterodimerization capacity and its functional effects on cell wall architecture, cellulose crystallinity, and saccharification efficiency remains unclear. Here, we reported the highly potent binding site containing four residues of Pro435, Trp436, Pro437, and Gly438 in the plant‐conserved region (P‐CR) of PalCESA4 subunit, which are involved in the CESA4‐CESA8 heterodimerization. The CRISPR/Cas9‐knockout mutagenesis in the predicted binding site results in physiological abnormalities, stunt growth …