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RNA-binding properties of an unusual ribosomal protein TL5 from Thermus thermophilus.
Biochemistry (Mosc). 1997 May; 62(5):537-42.B

Abstract

The gene encoding the 5S rRNA-binding ribosomal protein TL5 from Thermus thermophilus, an extremely thermophilic species, was expressed in E. coli. A method for isolation of TL5 from the overproducing strain was developed. Samples of TL5 protein isolated from ribosomes and the overproducing strain displayed identical RNA-binding properties. Circular dichroic spectroscopy was used to calculate the secondary structure of the protein. TL5 was shown to form a stable complex with the 3'-terminal fragment of 5S rRNA, which is similar to the fragment of E. coli RNA that binds to L25 protein. The data suggest that TL5 from T. thermophilus and L25 from E. coli bind to similar sites on the 5S rRNA molecule.

Authors+Show Affiliations

Meshcheryakov VA
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.
Gryaznova OI
No affiliation info available
Davydova NL
No affiliation info available
Mudrik ES
No affiliation info available
Perederina AA
No affiliation info available
Vasilenko NL
No affiliation info available
Gongadze GM
No affiliation info available
Garber MB
No affiliation info available

MeSH

Bacterial ProteinsBinding SitesCircular DichroismEscherichia coliRNA-Binding ProteinsRecombinant ProteinsRibosomal ProteinsThermus thermophilus

Pub Type(s)

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

Language

eng

PubMed ID

9275294

Citation

Meshcheryakov, V A., et al. "RNA-binding Properties of an Unusual Ribosomal Protein TL5 From Thermus Thermophilus." Biochemistry. Biokhimiia, vol. 62, no. 5, 1997, pp. 537-42.
Meshcheryakov VA, Gryaznova OI, Davydova NL, et al. RNA-binding properties of an unusual ribosomal protein TL5 from Thermus thermophilus. Biochemistry (Mosc). 1997;62(5):537-42.
Meshcheryakov, V. A., Gryaznova, O. I., Davydova, N. L., Mudrik, E. S., Perederina, A. A., Vasilenko, N. L., Gongadze, G. M., & Garber, M. B. (1997). RNA-binding properties of an unusual ribosomal protein TL5 from Thermus thermophilus. Biochemistry. Biokhimiia, 62(5), 537-42.
Meshcheryakov VA, et al. RNA-binding Properties of an Unusual Ribosomal Protein TL5 From Thermus Thermophilus. Biochemistry (Mosc). 1997;62(5):537-42. PubMed PMID: 9275294.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - RNA-binding properties of an unusual ribosomal protein TL5 from Thermus thermophilus. AU - Meshcheryakov,V A, AU - Gryaznova,O I, AU - Davydova,N L, AU - Mudrik,E S, AU - Perederina,A A, AU - Vasilenko,N L, AU - Gongadze,G M, AU - Garber,M B, PY - 1997/5/1/pubmed PY - 1997/5/1/medline PY - 1997/5/1/entrez SP - 537 EP - 42 JF - Biochemistry. Biokhimiia JO - Biochemistry (Mosc) VL - 62 IS - 5 N2 - The gene encoding the 5S rRNA-binding ribosomal protein TL5 from Thermus thermophilus, an extremely thermophilic species, was expressed in E. coli. A method for isolation of TL5 from the overproducing strain was developed. Samples of TL5 protein isolated from ribosomes and the overproducing strain displayed identical RNA-binding properties. Circular dichroic spectroscopy was used to calculate the secondary structure of the protein. TL5 was shown to form a stable complex with the 3'-terminal fragment of 5S rRNA, which is similar to the fragment of E. coli RNA that binds to L25 protein. The data suggest that TL5 from T. thermophilus and L25 from E. coli bind to similar sites on the 5S rRNA molecule. SN - 0006-2979 UR - https://www.unboundmedicine.com/medline/citation/9275294/RNA_binding_properties_of_an_unusual_ribosomal_protein_TL5_from_Thermus_thermophilus_ DB - PRIME DP - Unbound Medicine ER -