A ribosomal protein from Thermus thermophilus is homologous to a general shock protein.
The gene encoding the ribosomal protein from Thermus thermophilus, TL5, which binds to the 5S rRNA, has been cloned and sequenced. The codon usage shows a clear preference for G/C rich codons that is characteristic for many genes in thermophilic bacteria. The deduced amino acid sequence consists of 206 residues. The sequence of TL5 shows a strong similarity to a general shock protein from Bacillus subtilis, named CTC. The protein CTC is homologous in its N-terminal part to the 5S rRNA binding protein, L25, from E coli. An alignment of the TL5, CTC and L25 sequences displays a number of residues that are totally conserved. No clear sequence similarity was found between TL5 and other proteins which are known to bind to 5S rRNA. The evolutionary relationship of a heat shock protein in mesophiles and a ribosomal protein in thermophilic bacteria as well as a possible role of TL5 in the ribosome are discussed.
Gryaznova
O I
OI
Center of Chemistry and Chemical Engineering, Lund University, Sweden.
Davydova
N L
NL
Gongadze
G M
GM
Jonsson
B H
BH
Garber
M B
MB
Liljas
A
A
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000378:metabolism; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry; D001483:Base Sequence; D003062:Codon; D004926:Escherichia coli / Q000378:metabolism; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D012341:RNA, Ribosomal, 5S / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000096:biosynthesis* / Q000737:chemistry; D012269:Ribosomal Proteins / Q000096:biosynthesis* / Q000737:chemistry; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D016963:Thermus thermophilus / Q000378:metabolism*
D001426:Bacterial Proteins; D003062:Codon; D012341:RNA, Ribosomal, 5S; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins; C106696:TL5 protein, Thermus thermophilus; C106697:protein CTC, Bacteria; C031127:ribosomal protein L25