Zengel J M, Epstein H F
Proc Natl Acad Sci U S A. 1980 Feb;77(2):852-6. doi: 10.1073/pnas.77.2.852.
Mutations in the unc-52 gene on linkage group II retard the construction of body-wall muscle sarcomeres during larval development in the nematode Caenorhabditis elegans. Unc-52 mutants show decreased accumulation of myosin heavy chains relative to other polypeptides during larval development, correlating with the structural retardation. Pulse radiolabeling experiments show that decreased synthesis of specific body-wall myosin heavy chains that are encoded by the unc-54 gene on linkage group I is responsible for the defective myosin accumulation. In the wild type, a constant ratio of the synthesis of the unc-54-coded myosin B to myosin A, about 2:1, is maintained during the larval stages in which the synthesis of both myosins increases exponentially and rapid sarcomere growth and addition ensues. During the first 26 hr of larval development, before any structural or behavioral effects of unc-52 mutations are apparent, the synthesis of myosin heavy chains is also normal. By 38 hr, decreased synthesis of myosin B is detected in the unc-52 mutant SU200, when sarcomere growth slows considerably. The effects of mutation in the unc-52 locus are trans acting upon the synthesis of unc-54-coded myosin in a specific set of muscle cells during a defined period of larval development.
秀丽隐杆线虫连锁群II上unc-52基因的突变会阻碍幼虫发育期间体壁肌肉肌节的构建。在幼虫发育过程中,相对于其他多肽,unc-52突变体中肌球蛋白重链的积累减少,这与结构发育迟缓相关。脉冲放射性标记实验表明,连锁群I上unc-54基因编码的特定体壁肌球蛋白重链合成减少是肌球蛋白积累缺陷的原因。在野生型中,在幼虫阶段,unc-54编码的肌球蛋白B与肌球蛋白A的合成保持恒定比例,约为2:1,在此期间,两种肌球蛋白的合成呈指数增长,随后肌节迅速生长并增加。在幼虫发育的前26小时,在unc-52突变的任何结构或行为影响显现之前,肌球蛋白重链的合成也是正常的。到38小时时,在unc-52突变体SU200中检测到肌球蛋白B的合成减少,此时肌节生长显著减缓。unc-52位点的突变效应在幼虫发育的特定时期对一组特定肌肉细胞中unc-54编码的肌球蛋白合成起反式作用。