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一个水稻微管酪氨酸连接酶样蛋白 12 影响微管的动态和取向。

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

机构信息

Molecular Cell Biology, Botanical Institute, Karlsruhe Institute of Technology, Karlsruhe, 76131, Germany.

Aptamer Initiative, Postech Biotech Center, Pohang University of Science and Technology, Pohang-si, Gyeongsangbuk-do, 37673, South Korea.

出版信息

J Integr Plant Biol. 2021 May;63(5):848-864. doi: 10.1111/jipb.13059. Epub 2021 Mar 19.

Abstract

The detyrosination/retyrosination cycle is the most common post-translational modification of α-tubulin. Removal 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 (OsTTLL12) and generated overexpression OsTTLL12-RFP lines in both rice and tobacco BY-2 cells. We found, unexpectedly, that overexpression of this OsTTLL12-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 OsTTLL12 overexpression affects structural and dynamic features of microtubules, followed by changes in the axiality of cell plate deposition and, consequently, plant growth.

摘要

去酪氨酸化/再酪氨酸化循环是α-微管蛋白最常见的翻译后修饰。通过一种尚未被揭示的微管酪氨酸羧肽酶从α-微管蛋白保守的 C 端酪氨酸上除去,然后通过微管酪氨酸连接酶(TTL)重新连接这个酪氨酸,这可能是所有真核生物共有的。有趣的是,对于植物来说,唯一有资格作为潜在 TTL 同源物的候选物是微管酪氨酸连接酶样 12 蛋白。为了深入了解这些潜在 TTL 同源物的生物学功能,我们克隆了水稻 TTL 样 12 蛋白(OsTTLL12),并在水稻和烟草 BY-2 细胞中生成了过表达 OsTTLL12-RFP 的系。出乎意料的是,我们发现过表达这种 OsTTLL12-RFP 增加了 coleoptile 和 seminal root 中去酪氨酸化的α-微管蛋白的相对丰度,与更稳定的微管相关。这与皮质微管的各自取向无关,并伴随着 coleoptiles 和 seminal roots 的相应生长变化。分裂期微管组织的紊乱和细胞壁的定向紊乱是这种表型的进一步特征。因此,由于 OsTTLL12 过表达导致的微管去酪氨酸化升高会影响微管的结构和动态特性,随后改变细胞板沉积的轴向性,从而影响植物生长。

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