Westermann S, Weber K
Max Planck Institute for Biophysical Chemistry, Department of Biochemistry, Am Fassberg 11, 37077, Göttingen, Germany.
Biochim Biophys Acta. 2000 Jul 24;1492(2-3):483-7. doi: 10.1016/s0167-4781(00)00113-5.
We report the isolation, cloning and recombinant expression of a Trypanosoma brucei homolog of the La RNA-binding protein. Based on peptide sequence information we have isolated a cDNA clone which encodes a protein of 335 amino acids with a predicted molecular weight of 37.7 kDa. The amino acid sequence fits the domain structure of known La proteins and contains a putative ATP-binding site located in the COOH-terminal domain. The cDNA was expressed as a glutathione S-transferase fusion protein in Escherichia coli, and the recombinant protein displayed RNA-binding activity in an electrophoretic mobility shift assay.
我们报道了布氏锥虫La RNA结合蛋白同源物的分离、克隆及重组表达。基于肽序列信息,我们分离出一个cDNA克隆,它编码一个由335个氨基酸组成的蛋白质,预测分子量为37.7 kDa。该氨基酸序列符合已知La蛋白的结构域结构,并在COOH末端结构域含有一个推定的ATP结合位点。该cDNA在大肠杆菌中作为谷胱甘肽S-转移酶融合蛋白表达,并且重组蛋白在电泳迁移率变动分析中显示出RNA结合活性。