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[RNA-binding properties of ribosomal protein L1 from Thermus thermophilus].
Biokhimiia. 1996 Nov; 61(11):2040-4.B

Abstract

Fragments of the ribosomal protein L1 from Thermus thermophilus were obtained by limited trypsinolysis and spontaneous proteolysis. Binding of the intact L1 and its proteolytic fragments to 23S ribosomal RNA was studied. First eight N-terminal amino acids are important for RNA binding because protein L1 lacking these amino acids exhibits reduced 23S rRNA binding. Additional cleavage of the polypeptide chain between residues 36 and 37 completely abolishes RNA binding. Comparison of these data with recently determined structure of protein L1 from T. thermophilus suggests the nature of interactions which can determine specific and strong association of the protein L1 with 23S rRNA.

Authors

Elisekina IA
No affiliation info available
Avliiakulov NK
No affiliation info available
Grishkovskaia IB
No affiliation info available
Muranova TA
No affiliation info available
Sedel'nikova SE
No affiliation info available
Garber MB
No affiliation info available

MeSH

Amino Acid SequenceBacterial ProteinsMolecular Sequence DataRNA, BacterialRNA-Binding ProteinsRibosomal ProteinsThermus thermophilus

Pub Type(s)

English Abstract
Journal Article

Language

rus

PubMed ID

9004863

Citation

Elisekina, I A., et al. "[RNA-binding Properties of Ribosomal Protein L1 From Thermus Thermophilus]." Biokhimiia (Moscow, Russia), vol. 61, no. 11, 1996, pp. 2040-4.
Elisekina IA, Avliiakulov NK, Grishkovskaia IB, et al. [RNA-binding properties of ribosomal protein L1 from Thermus thermophilus]. Biokhimiia. 1996;61(11):2040-4.
Elisekina, I. A., Avliiakulov, N. K., Grishkovskaia, I. B., Muranova, T. A., Sedel'nikova, S. E., & Garber, M. B. (1996). [RNA-binding properties of ribosomal protein L1 from Thermus thermophilus]. Biokhimiia (Moscow, Russia), 61(11), 2040-4.
Elisekina IA, et al. [RNA-binding Properties of Ribosomal Protein L1 From Thermus Thermophilus]. Biokhimiia. 1996;61(11):2040-4. PubMed PMID: 9004863.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - [RNA-binding properties of ribosomal protein L1 from Thermus thermophilus]. AU - Elisekina,I A, AU - Avliiakulov,N K, AU - Grishkovskaia,I B, AU - Muranova,T A, AU - Sedel'nikova,S E, AU - Garber,M B, PY - 1996/11/1/pubmed PY - 1996/11/1/medline PY - 1996/11/1/entrez SP - 2040 EP - 4 JF - Biokhimiia (Moscow, Russia) JO - Biokhimiia VL - 61 IS - 11 N2 - Fragments of the ribosomal protein L1 from Thermus thermophilus were obtained by limited trypsinolysis and spontaneous proteolysis. Binding of the intact L1 and its proteolytic fragments to 23S ribosomal RNA was studied. First eight N-terminal amino acids are important for RNA binding because protein L1 lacking these amino acids exhibits reduced 23S rRNA binding. Additional cleavage of the polypeptide chain between residues 36 and 37 completely abolishes RNA binding. Comparison of these data with recently determined structure of protein L1 from T. thermophilus suggests the nature of interactions which can determine specific and strong association of the protein L1 with 23S rRNA. SN - 0320-9725 UR - https://www.unboundmedicine.com/medline/citation/9004863/[RNA_binding_properties_of_ribosomal_protein_L1_from_Thermus_thermophilus]_ DB - PRIME DP - Unbound Medicine ER -