Myosin I mutants with only 1% of wild-type actin-activated MgATPase activity retain essential in vivo function(s)
Myosin I mutants with only 1% of wild-type actin-activated MgATPase activity retain essential in vivo function(s)
复制标题
DOI：
10.1073/pnas.161285698
复制
发表时间：
2001-07
影响因子：
11.1
通讯作者：
Xiong Liu;N. Osherov;R. Yamashita;H. Brzeska;E. Korn;G. May
中科院分区：
文献类型：
--
作者：
Xiong Liu;N. Osherov;R. Yamashita;H. Brzeska;E. Korn;G. May
单I类肌球蛋白（MYOA）对细粒曲霉菌丝的生长至关重要。一般认为，所有肌凝蛋白的功能取决于它们的肌动蛋白激活的MgATPase活性。在这里，我们发现MYOA突变体在体外具有不超过野生型MYOA的1%的肌动蛋白激活的MgATPase活性，并且没有可检测到的体外运动活性，可以支持真菌细胞生长，尽管发芽时间延迟和菌丝伸长减少。从这些和其他数据，我们得出结论，肌凝蛋白I在A. nidulans中的基本作用可能是结构性的，如果有的话，它几乎不需要肌动蛋白激活的MgATPase或运动活性，而这些一直被认为是肌凝蛋白家族的定义特征。
The single class I myosin (MYOA) of Aspergillus nidulans is essential for hyphal growth. It is generally assumed that the functions of all myosins depend on their actin-activated MgATPase activity. Here we show that MYOA mutants with no more than 1% of the actin-activated MgATPase activity of wild-type MYOA in vitro and no detectable in vitro motility activity can support fungal cell growth, albeit with a delay in germination time and a reduction in hyphal elongation. From these and other data, we conclude that the essential role(s) of myosin I in A. nidulans is probably structural, requiring little, if any, actin-activated MgATPase or motor activity, which have long been considered the defining characteristics of the myosin family.