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

FEBS Lett. 1999 May 14;451(1):51-5. doi: 10.1016/s0014-5793(99)00538-4.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / metabolism*
  • Binding Sites
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • RNA, Ribosomal, 5S / chemistry
  • RNA, Ribosomal, 5S / metabolism*
  • RNA-Binding Proteins / metabolism*
  • Ribosomal Proteins / metabolism*
  • Sequence Homology, Amino Acid
  • Thermus thermophilus / metabolism*

Substances

  • Bacterial Proteins
  • RNA, Ribosomal, 5S
  • RNA-Binding Proteins
  • Ribosomal Proteins
  • TL5 protein, Thermus thermophilus