Institute of Botany 1 and Center for Functional Nanostructures, University of Karlsruhe, Kaiserstrasse 2, D-76128 Karlsruhe, Germany.
J Exp Bot. 2010 Mar;61(3):901-9. doi: 10.1093/jxb/erp369. Epub 2009 Dec 16.
Virtually all eukaryotic alpha-tubulins harbour a C-terminal tyrosine that can be reversibly removed and religated, catalysed by a specific tubulin-tyrosine carboxypeptidase (TTC) and a specific tubulin-tyrosine ligase (TTL), respectively. The biological function of this post-translational modification has remained enigmatic. 3-nitro-L-tyrosine (nitrotyrosine, NO(2)Tyr), can be incorporated into detyrosinated alpha-tubulin instead of tyrosine, producing irreversibly nitrotyrosinated alpha-tubulin. To gain insight into the possible function of detyrosination, the effect of NO(2)Tyr has been assessed in two plant model organisms (rice and tobacco). NO(2)Tyr causes a specific, sensitive, and dose-dependent inhibition of cell division that becomes detectable from 1 h after treatment and which is not observed with non-nitrosylated tyrosine. These effects are most pronounced in cycling tobacco BY-2 cells, where the inhibition of cell division is accompanied by a stimulation of cell length, and a misorientation of cross walls. NO(2)Tyr reduces the abundance of the detyrosinated form of alpha-tubulin whereas the tyrosinated alpha-tubulin is not affected. These findings are discussed with respect to a model where NO(2)Tyr is accepted as substrate by TTL and subsequently blocks TTC activity. The irreversibly tyrosinated alpha-tubulin impairs microtubular functions that are relevant to cell division in general, and cell wall deposition in particular.
基本上所有真核生物的α-微管蛋白都带有一个 C 末端的酪氨酸,这个酪氨酸可以被一个特定的微管蛋白-酪氨酸羧肽酶(TTC)和一个特定的微管蛋白-酪氨酸连接酶(TTL)可逆地去除和重新连接。这个翻译后修饰的生物学功能一直是个谜。3-硝基-L-酪氨酸(硝基酪氨酸,NO2Tyr)可以取代酪氨酸掺入去酪氨酸化的α-微管蛋白中,产生不可逆的硝基酪氨酸化的α-微管蛋白。为了深入了解去酪氨酸化的可能功能,我们在两种植物模式生物(水稻和烟草)中评估了 NO2Tyr 的作用。NO2Tyr 会特异性、敏感地、剂量依赖性地抑制细胞分裂,这种抑制作用在处理后 1 小时即可检测到,而非硝基化的酪氨酸则不会产生这种作用。在有丝分裂的烟草 BY-2 细胞中,这种抑制作用最为明显,细胞分裂受到抑制的同时伴随着细胞长度的增加和细胞壁交叉的错位。NO2Tyr 降低了去酪氨酸化α-微管蛋白的丰度,而酪氨酸化的α-微管蛋白不受影响。这些发现与一个模型有关,该模型认为 NO2Tyr 被 TTL 接受为底物,随后阻止了 TTC 的活性。不可逆的酪氨酸化的α-微管蛋白会损害与细胞分裂一般相关、特别是与细胞壁沉积相关的微管功能。