5S rRNA binding ribosomal proteins from Thermus thermophilus: identification and some structural properties.
An unusual acidic ribosomal protein from Thermus thermophilus, TL5, that binds to 5S rRNA specifically and strongly, has been investigated. The N-terminal sequence of TL5 does not reveal any homology with known ribosomal proteins. Two large tryptic fragments of TL5 have been isolated and characterized. 5S rRNA protected TL5 and its unstable N-terminal fragment against trypsin action. The 5S rRNA binding ability of TL5 is probably inherent in its N-terminal part. The other 5S rRNA binding ribosomal protein from T. thermophilus, TL4, has been identified as a homolog of the ribosomal protein L5 from Escherichia coli.
Gongadze
G
G
Department of Structure and Function of Ribosomes, Institute of Protein Research, Russian Academy of Sciences, Moscow Region, Russian Federation.
Kashparov
I
I
Lorenz
S
S
Schroeder
W
W
Erdmann
V A
VA
Liljas
A
A
Garber
M
M
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012341:RNA, Ribosomal, 5S / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D016963:Thermus thermophilus / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism
D001426:Bacterial Proteins; D012341:RNA, Ribosomal, 5S; D012269:Ribosomal Proteins; D014357:Trypsin