Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
The Thermus thermophilus 5S rRNA-protein complex : Identification of specific binding sites for proteins L5 and L18 in the 5S rRNA. / Gongadze, G. M.; Perederina, A. A.; Meshcheryakov, V. A.; Fedorov, R. V.; Moskalenko, S. E.; Rak, A. V.; Serganov, A. A.; Shcherbakov, D. V.; Nikonov, S. V.; Garber, M. B.
в: Molecular Biology, Том 35, № 4, 01.07.2001, стр. 521-526.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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TY - JOUR
T1 - The Thermus thermophilus 5S rRNA-protein complex
T2 - Identification of specific binding sites for proteins L5 and L18 in the 5S rRNA
AU - Gongadze, G. M.
AU - Perederina, A. A.
AU - Meshcheryakov, V. A.
AU - Fedorov, R. V.
AU - Moskalenko, S. E.
AU - Rak, A. V.
AU - Serganov, A. A.
AU - Shcherbakov, D. V.
AU - Nikonov, S. V.
AU - Garber, M. B.
PY - 2001/7/1
Y1 - 2001/7/1
N2 - 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 Å. 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.
AB - 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 Å. 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.
KW - 5S rRNA
KW - Bacterial ribosome
KW - Ribosomal proteins
KW - RNA-protein interactions
KW - Thermus thermophilus
UR - http://www.scopus.com/inward/record.url?scp=18044392538&partnerID=8YFLogxK
U2 - 10.1023/A:1010562707875
DO - 10.1023/A:1010562707875
M3 - Article
AN - SCOPUS:18044392538
VL - 35
SP - 521
EP - 526
JO - Molecular Biology
JF - Molecular Biology
SN - 0026-8933
IS - 4
ER -
ID: 47465529