Yazu M, Adachi H, Sutoh K
Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, 3-8-1 Komaba, Meguro-ku, Tokyo, 153-8902, Japan.
Biochem Biophys Res Commun. 1999 Feb 24;255(3):711-6. doi: 10.1006/bbrc.1999.0264.
We have identified and sequenced a novel unconventional myosin termed MyoK in Dictyostelium. Like class XIV myosins, MyoK has a very short and basic tail and lacks light chain-binding IQ motifs. In contrast, a phylogenetic analysis of the motor domain (head) clearly indicated that MyoK belongs to class I myosins. Surprisingly, at the loop-1 site of the head, an insert of 142 amino acid residues was found, the longest in all myosins so far sequenced. The insert was rich in Gly and Pro and could serve as a secondary actin-binding site, as is the case with those present in the tail of some class I myosins. The expression of the MyoK transcript was stimulated at very early stages of Dictyostelium development. The growth and terminal developmental phenotype of the Dictyostelium cell were not affected by the myoK- mutation, suggesting the existence of myosin(s) with functions overlapping those of MyoK.
我们在盘基网柄菌中鉴定并测序了一种名为MyoK的新型非常规肌球蛋白。与十四类肌球蛋白一样,MyoK具有非常短且呈碱性的尾部,并且缺乏轻链结合IQ基序。相比之下,对运动结构域(头部)的系统发育分析清楚地表明,MyoK属于一类肌球蛋白。令人惊讶的是,在头部的环1位点发现了一个142个氨基酸残基的插入序列,这是迄今为止所有已测序的肌球蛋白中最长的。该插入序列富含甘氨酸和脯氨酸,并且可以作为第二个肌动蛋白结合位点,就像一些一类肌球蛋白尾部中的那些位点一样。MyoK转录本的表达在盘基网柄菌发育的非常早期阶段受到刺激。盘基网柄菌细胞的生长和终末发育表型不受myoK突变的影响,这表明存在功能与MyoK重叠的肌球蛋白。