RNA-binding properties of an unusual ribosomal protein TL5 from Thermus thermophilus.
The gene encoding the 5S rRNA-binding ribosomal protein TL5 from Thermus thermophilus, an extremely thermophilic species, was expressed in E. coli. A method for isolation of TL5 from the overproducing strain was developed. Samples of TL5 protein isolated from ribosomes and the overproducing strain displayed identical RNA-binding properties. Circular dichroic spectroscopy was used to calculate the secondary structure of the protein. TL5 was shown to form a stable complex with the 3'-terminal fragment of 5S rRNA, which is similar to the fragment of E. coli RNA that binds to L25 protein. The data suggest that TL5 from T. thermophilus and L25 from E. coli bind to similar sites on the 5S rRNA molecule.
Meshcheryakov
V A
VA
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.
Gryaznova
O I
OI
Davydova
N L
NL
Mudrik
E S
ES
Perederina
A A
AA
Vasilenko
N L
NL
Gongadze
G M
GM
Garber
M B
MB
D001426:Bacterial Proteins; D001665:Binding Sites; D002942:Circular Dichroism; D004926:Escherichia coli / Q000235:genetics; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D012269:Ribosomal Proteins / Q000235:genetics / Q000378:metabolism*; D016963:Thermus thermophilus / Q000378:metabolism*
D001426:Bacterial Proteins; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins; D012269:Ribosomal Proteins; C106696:TL5 protein, Thermus thermophilus