Sanders G, Lichte B, Meyer H E, Kilimann M W
Institut für Physiologische Chemie, Ruhr-Universität Bochum, Germany.
FEBS Lett. 1992 Oct 26;311(3):295-8. doi: 10.1016/0014-5793(92)81123-4.
We report the cDNA-deduced primary structure of the chicken counterpart of the murine dilute gene product, a member of the myosin I family. Comparison of the chicken and mouse sequences reveals a distinct pattern of domains of high and low sequence conservation. An internal deletion of 25 amino acids probably reflects differential mRNA processing. Compared with other myosin heavy chain molecules, sequence similarity is highest with the MYO2 gene product of Saccharomyces cerevisiae. The MYO2 protein, implicated in vectorial vesicle transport, is homologous to the dilute protein over practically its entire length. In addition, the C-terminal domain of the dilute protein is highly similar to a putative glutamic acid decarboxylase sequence cloned from mouse brain. Alternatively, this closely related clone might represent an isoform of the dilute protein derived from a second gene, potentially involved in genetic conditions related to dilute.
我们报道了小鼠稀释基因产物（肌球蛋白I家族成员）的鸡对应物的cDNA推导的一级结构。鸡和小鼠序列的比较揭示了高序列保守和低序列保守结构域的独特模式。25个氨基酸的内部缺失可能反映了不同的mRNA加工过程。与其他肌球蛋白重链分子相比，与酿酒酵母的MYO2基因产物的序列相似性最高。参与向量囊泡运输的MYO2蛋白在几乎整个长度上与稀释蛋白同源。此外，稀释蛋白的C末端结构域与从小鼠脑克隆的推定谷氨酸脱羧酶序列高度相似。或者，这个密切相关的克隆可能代表来自第二个基因的稀释蛋白的同工型，可能与稀释相关的遗传条件有关。
