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.
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.
Gongadze
G M
GM
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region. gongadze@vega.protres.ru
Meshcheryakov
V A
VA
Serganov
A A
AA
Fomenkova
N P
NP
Mudrik
E S
ES
Jonsson
B H
BH
Liljas
A
A
Nikonov
S V
SV
Garber
M B
MB
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D012341:RNA, Ribosomal, 5S / Q000737:chemistry / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D016963:Thermus thermophilus / Q000378:metabolism*
D001426:Bacterial Proteins; D012341:RNA, Ribosomal, 5S; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins; C106696:TL5 protein, Thermus thermophilus