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Ribosomal proteins, TL4 and TL5, from Thermus thermophilus form hybrid complexes with 5 S ribosomal RNA from different microorganisms
Author(s) -
Gongadze G.M.,
Tishchenko S.V.,
Sedelnikova S.E.,
Garber M.B.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80916-i
Subject(s) - thermus thermophilus , ribosomal protein , ribosomal rna , 5s ribosomal rna , 28s ribosomal rna , rna , 5.8s ribosomal rna , 18s ribosomal rna , 50s , biochemistry , biology , ribosome , eukaryotic large ribosomal subunit , 30s , escherichia coli , microbiology and biotechnology , chemistry , gene
Hybrid complexes of the ribosomal proteins, TL4 and TL5, from Thermus thermophilus with 5 S ribosomal RNA from Escherichia coli and Bacillus stearothermophilus have been prepared. There was no competition between the two proteins for the binding sites. Stoichiometry of 5 S RNA binding for both proteins was 1:1 (protein/RNA). The TL4 protein competed with the E. coli ribosomal L5 protein, and the TL5 protein competed with the E. coli ribosomal proteins, L18 and L25, for binding with 5 S RNA.