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Domain II of Thermus thermophilus ribosomal protein L1 hinders recognition of its mRNA.
J Mol Biol. 2008 Nov 07; 383(2):301-5.JM

Abstract

The two-domain ribosomal protein L1 has a dual function as a primary rRNA-binding ribosomal protein and as a translational repressor that binds its own mRNA. Here, we report the crystal structure of a complex between the isolated domain I of L1 from the bacterium Thermus thermophilus and a specific mRNA fragment from Methanoccocus vannielii. In parallel, we report kinetic characteristics measured for complexes formed by intact TthL1 and its domain I with the specific mRNA fragment. Although, there is a close similarity between the RNA-protein contact regions in both complexes, the association rate constant is higher in the case of the complex formed by the isolated domain I. This finding demonstrates that domain II hinders mRNA recognition by the intact TthL1.

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Authors+Show Affiliations

Tishchenko S
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow region, Russia.
Kljashtorny V
No affiliation info available
Kostareva O
No affiliation info available
Nevskaya N
No affiliation info available
Nikulin A
No affiliation info available
Gulak P
No affiliation info available
Piendl W
No affiliation info available
Garber M
No affiliation info available
Nikonov S
No affiliation info available

MeSH

Amino Acid SequenceBacterial ProteinsBinding SitesCrystallography, X-RayKineticsMethanococcusModels, MolecularMolecular Sequence DataProtein Structure, TertiaryRNA, BacterialRNA, MessengerRibosomal ProteinsThermus thermophilus

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18778715

Citation

Tishchenko, Svetlana, et al. "Domain II of Thermus Thermophilus Ribosomal Protein L1 Hinders Recognition of Its MRNA." Journal of Molecular Biology, vol. 383, no. 2, 2008, pp. 301-5.
Tishchenko S, Kljashtorny V, Kostareva O, et al. Domain II of Thermus thermophilus ribosomal protein L1 hinders recognition of its mRNA. J Mol Biol. 2008;383(2):301-5.
Tishchenko, S., Kljashtorny, V., Kostareva, O., Nevskaya, N., Nikulin, A., Gulak, P., Piendl, W., Garber, M., & Nikonov, S. (2008). Domain II of Thermus thermophilus ribosomal protein L1 hinders recognition of its mRNA. Journal of Molecular Biology, 383(2), 301-5. https://doi.org/10.1016/j.jmb.2008.08.058
Tishchenko S, et al. Domain II of Thermus Thermophilus Ribosomal Protein L1 Hinders Recognition of Its MRNA. J Mol Biol. 2008 Nov 7;383(2):301-5. PubMed PMID: 18778715.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Domain II of Thermus thermophilus ribosomal protein L1 hinders recognition of its mRNA. AU - Tishchenko,Svetlana, AU - Kljashtorny,Vladislav, AU - Kostareva,Olga, AU - Nevskaya,Natalia, AU - Nikulin,Alexei, AU - Gulak,Pavel, AU - Piendl,Wolfgang, AU - Garber,Maria, AU - Nikonov,Stanislav, Y1 - 2008/08/29/ PY - 2008/07/29/received PY - 2008/08/19/accepted PY - 2008/9/10/pubmed PY - 2009/1/14/medline PY - 2008/9/10/entrez SP - 301 EP - 5 JF - Journal of molecular biology JO - J Mol Biol VL - 383 IS - 2 N2 - The two-domain ribosomal protein L1 has a dual function as a primary rRNA-binding ribosomal protein and as a translational repressor that binds its own mRNA. Here, we report the crystal structure of a complex between the isolated domain I of L1 from the bacterium Thermus thermophilus and a specific mRNA fragment from Methanoccocus vannielii. In parallel, we report kinetic characteristics measured for complexes formed by intact TthL1 and its domain I with the specific mRNA fragment. Although, there is a close similarity between the RNA-protein contact regions in both complexes, the association rate constant is higher in the case of the complex formed by the isolated domain I. This finding demonstrates that domain II hinders mRNA recognition by the intact TthL1. SN - 1089-8638 UR - https://www.unboundmedicine.com/medline/citation/18778715/Domain_II_of_Thermus_thermophilus_ribosomal_protein_L1_hinders_recognition_of_its_mRNA_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(08)01066-8 DB - PRIME DP - Unbound Medicine ER -