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嗜热栖热菌的一种核糖体蛋白与一种通用应激蛋白同源。

A ribosomal protein from Thermus thermophilus is homologous to a general shock protein.

作者信息

Gryaznova O I, Davydova N L, Gongadze G M, Jonsson B H, Garber M B, Liljas A

机构信息

Center of Chemistry and Chemical Engineering, Lund University, Sweden.

出版信息

Biochimie. 1996;78(11-12):915-9. doi: 10.1016/s0300-9084(97)86713-2.

Abstract

The gene encoding the ribosomal protein from Thermus thermophilus, TL5, which binds to the 5S rRNA, has been cloned and sequenced. The codon usage shows a clear preference for G/C rich codons that is characteristic for many genes in thermophilic bacteria. The deduced amino acid sequence consists of 206 residues. The sequence of TL5 shows a strong similarity to a general shock protein from Bacillus subtilis, named CTC. The protein CTC is homologous in its N-terminal part to the 5S rRNA binding protein, L25, from E coli. An alignment of the TL5, CTC and L25 sequences displays a number of residues that are totally conserved. No clear sequence similarity was found between TL5 and other proteins which are known to bind to 5S rRNA. The evolutionary relationship of a heat shock protein in mesophiles and a ribosomal protein in thermophilic bacteria as well as a possible role of TL5 in the ribosome are discussed.

摘要

编码嗜热栖热菌核糖体蛋白TL5(该蛋白与5S rRNA结合)的基因已被克隆并测序。密码子使用情况显示出对富含G/C的密码子有明显偏好,这是嗜热细菌中许多基因的特征。推导的氨基酸序列由206个残基组成。TL5的序列与枯草芽孢杆菌的一种通用应激蛋白CTC有很强的相似性。蛋白质CTC在其N端部分与来自大肠杆菌的5S rRNA结合蛋白L25同源。TL5、CTC和L25序列的比对显示出许多完全保守的残基。在TL5与其他已知与5S rRNA结合的蛋白质之间未发现明显的序列相似性。讨论了嗜温菌中的热休克蛋白与嗜热细菌中的核糖体蛋白之间的进化关系以及TL5在核糖体中的可能作用。

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