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  • Title: N-terminal domain, residues 1-91, of ribosomal protein TL5 from Thermus thermophilus binds specifically and strongly to the region of 5S rRNA containing loop E.
    Author: Gongadze GM, Meshcheryakov VA, Serganov AA, Fomenkova NP, Mudrik ES, Jonsson BH, Liljas A, Nikonov SV, Garber MB.
    Journal: FEBS Lett; 1999 May 14; 451(1):51-5. PubMed ID: 10356982.
    Abstract:
    In this work we show for the first time that the overproduced N-terminal fragment (residues 1-91) of ribosomal protein TL5 binds specifically to 5S rRNA and that the region of this fragment containing residues 80-91 is a necessity for its RNA-binding activity. The fragment of Escherichia coli 5S rRNA protected by TL5 against RNase A hydrolysis was isolated and sequenced. This 39 nucleotides fragment contains loop E and helices IV and V of 5S rRNA. The isolated RNA fragment forms stable complexes with TL5 and its N-terminal domain. Crystals of TL5 in complex with the RNA fragment diffracting to 2.75 A resolution were obtained.
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