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

G. M. Gongadze; A. A. Perederina; V. A. Meshcheryakov; R. V. Fedorov; S. E. Moskalenko; A. V. Rak; A. A. Serganov; D. V. Shcherbakov; S. V. Nikonov; M. B. Garber

doi:10.1023/A:1010562707875

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

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

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

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 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.

Original language	English (US)
Pages (from-to)	521-526
Number of pages	6
Journal	Molecular Biology
Volume	35
Issue number	4
DOIs	https://doi.org/10.1023/A:1010562707875
State	Published - Jul 2001

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology

Access to Document

10.1023/A:1010562707875

Cite this

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. (2001). The Thermus thermophilus 5S rRNA-protein complex: Identification of specific binding sites for proteins L5 and L18 in the 5S rRNA. Molecular Biology, 35(4), 521-526. https://doi.org/10.1023/A:1010562707875

@article{16974d443c5d454db0325ca780821201,

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

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 {\AA}. 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.",

author = "Gongadze, {G. M.} and Perederina, {A. A.} and Meshcheryakov, {V. A.} and Fedorov, {R. V.} and Moskalenko, {S. E.} and Rak, {A. V.} and Serganov, {A. A.} and Shcherbakov, {D. V.} and Nikonov, {S. V.} and Garber, {M. B.}",

note = "Funding Information: ACKNOWLEDGMENTS We are grateful to K.Kh. Lenskikh for synthesis of [14C]valine hydrazide and to E. Mudrik for technical assistance. This work was supported by the Russian Academy of Sciences and the Russian Foundation for Basic Research (project no. 98-04-48314). M.B. Gar-ber acknowledges a grant from Howard Hughes (55000308).",

year = "2001",

month = jul,

doi = "10.1023/A:1010562707875",

language = "English (US)",

volume = "35",

pages = "521--526",

journal = "Molecular Biology",

issn = "0026-8933",

publisher = "Maik Nauka-Interperiodica Publishing",

number = "4",

}

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.

N1 - Funding Information: ACKNOWLEDGMENTS We are grateful to K.Kh. Lenskikh for synthesis of [14C]valine hydrazide and to E. Mudrik for technical assistance. This work was supported by the Russian Academy of Sciences and the Russian Foundation for Basic Research (project no. 98-04-48314). M.B. Gar-ber acknowledges a grant from Howard Hughes (55000308).

PY - 2001/7

Y1 - 2001/7

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.

UR - http://www.scopus.com/inward/record.url?scp=18044392538&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=18044392538&partnerID=8YFLogxK

U2 - 10.1023/A:1010562707875

DO - 10.1023/A:1010562707875

M3 - Article

AN - SCOPUS:18044392538

SN - 0026-8933

VL - 35

SP - 521

EP - 526

JO - Molecular Biology

JF - Molecular Biology

IS - 4

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this