Haberland J, Gerke V
Max Planck Institute for Biophysical Chemistry, Department of Biochemistry, Göttingen, Germany.
FEBS Lett. 1995 Jan 3;357(2):173-7. doi: 10.1016/0014-5793(94)01353-3.
The amino acid sequence of Rna1p, a yeast protein implicated in the maturation and/or nucleocytoplasmic transport of RNA, is characterised by the presence of eight leucine-rich repeats (LLRs) as well as two intervening repeats of a different type and a highly acidic C-terminal region. Limited proteolysis of purified Rna1p expressed recombinantly in bacteria reveals that the C-terminal extension but not the region containing the two types of repeats is highly accessible to proteolytic attack and that the C-terminal region most likely harbours (a) low affinity Ca(2+)-binding site(s). These results are indicative of the domain structure of the Rna1p molecule, with the repeats and the C-terminal region being accessible for different interactions.
Rna1p是一种参与RNA成熟和/或核质运输的酵母蛋白，其氨基酸序列的特征是存在八个富含亮氨酸的重复序列（LLRs），以及两个不同类型的中间重复序列和一个高度酸性的C末端区域。对在细菌中重组表达的纯化Rna1p进行有限的蛋白酶解分析表明，C末端延伸区域而非包含两种重复序列的区域极易受到蛋白酶攻击，并且C末端区域很可能含有低亲和力的Ca(2+)结合位点。这些结果表明了Rna1p分子的结构域，其重复序列和C末端区域可用于不同的相互作用。
