嗜热栖热菌的5S rRNA结合核糖体蛋白：鉴定及一些结构特性

5S rRNA binding ribosomal proteins from Thermus thermophilus: identification and some structural properties.

作者信息

Gongadze G, Kashparov I, Lorenz S, Schroeder W, Erdmann V A, Liljas A, Garber M

机构信息

Department of Structure and Function of Ribosomes, Institute of Protein Research, Russian Academy of Sciences, Moscow Region, Russian Federation.

出版信息

FEBS Lett. 1996 May 20;386(2-3):260-2. doi: 10.1016/0014-5793(96)00457-7.

DOI:10.1016/0014-5793(96)00457-7

PMID:8647295

Abstract

An unusual acidic ribosomal protein from Thermus thermophilus, TL5, that binds to 5S rRNA specifically and strongly, has been investigated. The N-terminal sequence of TL5 does not reveal any homology with known ribosomal proteins. Two large tryptic fragments of TL5 have been isolated and characterized. 5S rRNA protected TL5 and its unstable N-terminal fragment against trypsin action. The 5S rRNA binding ability of TL5 is probably inherent in its N-terminal part. The other 5S rRNA binding ribosomal protein from T. thermophilus, TL4, has been identified as a homolog of the ribosomal protein L5 from Escherichia coli.

摘要

对嗜热栖热菌中一种不寻常的酸性核糖体蛋白TL5进行了研究，该蛋白能特异性且强烈地结合5S rRNA。TL5的N端序列与已知核糖体蛋白没有任何同源性。已分离并鉴定了TL5的两个大的胰蛋白酶片段。5S rRNA保护TL5及其不稳定的N端片段免受胰蛋白酶作用。TL5的5S rRNA结合能力可能存在于其N端部分。嗜热栖热菌的另一种结合5S rRNA的核糖体蛋白TL4已被鉴定为大肠杆菌核糖体蛋白L5的同源物。