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 characteri
stic for many genes in thermophilic bacteria. The deduced amino acid s
equence consists of 206 residues. The sequence of TL5 shows a strong s
imilarity 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 L2
5 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 thermophi
lic bacteria as well as a possible role of TL5 in the ribosome are dis
cussed.