Literature DB >> 11524947

[The Thermus thermophilus 5S rRNA-protein complex: Identifications of specific binding sites for proteins L5 and L18 in 5S rRNA].

G M Gongadze1, A A Perederina, V A Meshcheriakov, R V Fedorov, S E Moskalenko, A V Rak, A A Serganov, D V Shcherbakov, S V Nikonov, M B Garber.   

Abstract

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 A. 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.

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Year:  2001        PMID: 11524947

Source DB:  PubMed          Journal:  Mol Biol (Mosk)        ISSN: 0026-8984


  2 in total

1.  Biological significance of 5S rRNA import into human mitochondria: role of ribosomal protein MRP-L18.

Authors:  Alexandre Smirnov; Nina Entelis; Robert P Martin; Ivan Tarassov
Journal:  Genes Dev       Date:  2011-06-15       Impact factor: 11.361

2.  Protein L5 is crucial for in vivo assembly of the bacterial 50S ribosomal subunit central protuberance.

Authors:  Alexey P Korepanov; Anna V Korobeinikova; Sergey A Shestakov; Maria B Garber; George M Gongadze
Journal:  Nucleic Acids Res       Date:  2012-07-20       Impact factor: 16.971

  2 in total

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