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AtMAC stabilizes the phragmoplast by crosslinking microtubules and actin filaments during cytokinesis

Journal of Integrative Plant Biology 2023年第8期65卷 1950-1965页

作者： Pingzhou Du Yu Liu Lu Deng Dong Qian Xiuhua Xue Ting Yang Tonghui Li Yun Xiang Haiyun Ren Center for Biological Science and Technology Key Laboratory of Cell Proliferation and Regulation Biology of Ministry of EducationZhuhai-Macao Biotechnology Joint LaboratoryAdvanced Institute of Natural ScienceBeijing Normal UniversityZhuhai 519087China MOE Key Laboratory of Cell Activities and Stress Adaptations School of Life SciencesLanzhou UniversityLanzhou 73000oChina

The phragmoplast,a structure crucial for the completion of cytokinesis in plant cells,is composed of antiparallel microtubules(MTs)and actin filaments(AFs).However,how the parallel structure of phragmoplast MTs and AFs is maintained,especially during centrifugal phragmoplast expansion,remains ***,we analyzed a new Arabidopsis thaliana MT and AF crosslinking protein(AtMAC).When AtMAC was deleted,the phragmoplast showed disintegrity during centrifugal expansion,and the resulting phragmoplast fragmentation led to incomplete cell *** of AtMAC increased the resistance of phragmoplasts to depolymerization and caused the formation of additional phragmoplasts during *** experiments showed that AtMAC crosslinked MTs and AFs in vitro,and the truncated AtMAC protein,N-CC1,was the key domain controlling the ability of *** analysis showed that N-CC1(51–154)is the key domain for binding MTs,and N-CC1(51–125)for binding *** conclusion,AtMAC is the novel MT and AF crosslinking protein found to be involved in regulation of phragmoplast organization during centrifugal phragmoplast expansion,which is required for complete cytokinesis.

关键词： actin filaments AtMAC cytokinesis phragmoplast microtubules

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A rice tubulin tyrosine ligase-like 12 protein affects the dynamic and orientation of microtubules

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Journal of Integrative Plant Biology 2021年第5期63卷 848-864页

作者： Kunxi Zhang Xin Zhu Steffen Durst Petra Hohenberger Min‐Jung Han Gynheung An Vaidurya PSahi Michael Riemann Peter Nick Molecular Cell Biology Botanical InstituteKarlsruhe Institute of TechnologyKarlsruhe 76131Germany Aptamer Initiative Postech Biotech CenterPohang University of Science and TechnologyPohang‐siGyeongsangbuk‐do37673South Korea Department of Plant Molecular Systems Biotech Kyung Hee UniversityYongin 446‐701South Korea

The detyrosination/retyrosination cycle is the most common post-translational modification of α-*** of the conserved C-terminal tyrosine of α-tubulin by a still elusive tubulin tyrosine carboxypeptidase, and religation of this tyrosine by a tubulin tyrosine ligase(TTL), are probably common to all eukaryotes. Interestingly, for plants, the only candidates qualifying as potential TTL homologs are the tubulin tyrosine ligase-like 12 proteins. To get insight into the biological functions of these potential TTL homologs, we cloned the rice TTL-like 12 protein(Os TTLL12)andgeneratedoverexpression Os TTLL12-RFP lines in both rice and tobacco BY-2 cells. We found, unexpectedly, that overexpression of this Os TTLL12-RFP increased the relative abundance of detyrosinated α-tubulin in both coleoptile and seminal root, correlated with more stable microtubules. This was independent of the respective orientation of cortical microtubule, and followed by correspondingly changing growth of coleoptiles and seminal roots. A perturbed organization of phragmoplast microtubules and disoriented cell walls were further characteristics of this phenotype. Thus, the elevated tubulin detyrosination in consequence of Os TTLL12 overexpression affects structural and dynamic features of microtubules, followed by changes in the axiality of cell plate deposition and, consequently, plant growth.

关键词： microtubule phragmoplast rice tobacco BY-2 tubulin detyrosination tubulin tyrosine carboxypeptidase tubulin tyrosine ligase tubulin tyrosine ligase-like 12

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