The Thermus thermophilus 5S rRNA-protein complex:: Identification of specific binding sites for proteins L5 and L18 in the 5S rRNA

被引：8

作者：

Gongadze, GM ^{[1
]}

Perederina, AA ^{[1
]}

Meshcheryakov, VA ^{[1
]}

Fedorov, RV ^{[1
]}

Moskalenko, SE ^{[1
]}

Rak, AV ^{[1
]}

Serganov, AA ^{[1
]}

Shcherbakov, DV ^{[1
]}

Nikonov, SV ^{[1
]}

Garber, MB ^{[1
]}

机构：

[1] Russian Acad Sci, Inst Prot Res, Pushchino 142290, Moscow Region, Russia

来源：

MOLECULAR BIOLOGY | 2001年 / 35卷 / 04期

基金：

俄罗斯基础研究基金会;

关键词：

Thermus thermophilus; bacterial ribosome; 5S rRNA; ribosomal proteins; RNA-protein interactions;

D O I：

10.1023/A:1010562707875

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Three 5S rRNA-binding ribosomal proteins (L5, L18, TL5) of extremely thermophilic bacterium Thermus thermophilus have earlier been isolated. Structural analysis of their complexes with rRNA requires identification of their binding sites in the 5S rRNA. Previously, a TL5-binding site has been identified, a TL5-RNA complex crystallized, and its structure determined to 2.3 Angstrom. The sites for L5 and L18 were characterized, and two corresponding 5S rRNA fragments constructed. Of these, a 34-nt fragment specifically interacted with L5, and a 55-nt fragment interacted with L5, L18, and with both proteins. The 34-nt fragment-L5 complex was crystallized; the crystals are suitable for high-resolution X-ray analysis.

引用

页码：521 / 526

页数：6

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