286
P. TSIBOLI et al.
S. suI. gyrase
IYLFSCPNCGRSISTYRLLLGSVCNICLEE
: I
I: III: I II:: I : I III I
TthS14
Fig. 20.9. Alignment of the zinc-finger domain of TthS14, using the BLAST program, with the C4
zinc-finger domain of the S. sulfataricus gyrase-topoisomerase
human carcinomas (Fernandez-Pol 1993). Additionally, S27 from Entamoeba histolytica has been shown to bind Zn (Zhang 1993). The DNA-binding ability of the
S27 from eucaryotes raises the possibility that the members of the S14/S29 family
that contain a zinc-finger participate in a second function through interaction
with DNA sequences.
Interestingly, a search of the protein data banks for sequences that show high
homology to the zinc-finger motif of T. thermophilus S14 using the BLAST program
(Altschul et al. 1990) indicated great similarities between the TthS14 zinc-finger
domain and a C4 zinc-finger like motif in the amino-terminal (helicase) domain of
the reverse gyrases-topoisomerases (Confalonieri et al. 1993). The similarities are
obvious in the alignment of the Sulfolobus sulfataricus gyrase-topoisomerase and
the T. thermophilus S14 C4 zinc-finger domains (Fig. 20.9). There is an identity of 14
out of 30 amino acids and a similarity of an additional 6 amino acids.
In conclusion, the S14 ribosomal protein from T. thermophilus has been
proven to bind Zn in a molar ratio of one. This and the absolute requirement of
the protein structure for the binding of Zn indicate that the C4 motif of TthS14
participates in the formation of a zinc-finger domain. Additional experiments are
needed to elucidate the role the domain might play in the interaction of the
TthS14 protein with rRNA and/or DNA.
7
Acknowledgements
This work was supported by a grant from the General Secretariat of Reserach and
Technology. The authors wish to thank the Laboratory of Analytical Chemistry of
the Chemistry Department for the atomic absorption measurements and Prof.
Ada Yonath for interest and support in this work.
References
Altschul SF, Gish W, Miller W, Myers EW & Lipman DJ (1990) Basic local alignment search tool. J Mol
BioI 215: 403-410
Archer TK, Hager GL & Omichinski JG (1990) Sequence-specific DNA binding by glucocorticoid
receptor "zinc-finger peptides". Proc Nat! Acad Sci USA 87: 7560-7564
Auer J, Spieker G & Boeck A (1989) Organization and structure of the Methanococcus transcriptional
unit homologous to the E. coli "spectinomycin operon". Implications for the evolutionary relationship oOOS and 80S ribosomes. J Mol Bioi 209: 21-28
Chan YL, Suzuki K, Olvera J & Wool IG (1993) Zinc-finger-like motifs in rat ribosomal proteins S27
and S29. Nucl Acids Res 21(3): 649-655
Choli, T. (1989) Structural properties of ribosomal protein L11 from Escerichia coli. Biochem. Int. 19,
l323-l338
P. TSIBOLI et al.
S. suI. gyrase
IYLFSCPNCGRSISTYRLLLGSVCNICLEE
: I
I: III: I II:: I : I III I
TthS14
Fig. 20.9. Alignment of the zinc-finger domain of TthS14, using the BLAST program, with the C4
zinc-finger domain of the S. sulfataricus gyrase-topoisomerase
human carcinomas (Fernandez-Pol 1993). Additionally, S27 from Entamoeba histolytica has been shown to bind Zn (Zhang 1993). The DNA-binding ability of the
S27 from eucaryotes raises the possibility that the members of the S14/S29 family
that contain a zinc-finger participate in a second function through interaction
with DNA sequences.
Interestingly, a search of the protein data banks for sequences that show high
homology to the zinc-finger motif of T. thermophilus S14 using the BLAST program
(Altschul et al. 1990) indicated great similarities between the TthS14 zinc-finger
domain and a C4 zinc-finger like motif in the amino-terminal (helicase) domain of
the reverse gyrases-topoisomerases (Confalonieri et al. 1993). The similarities are
obvious in the alignment of the Sulfolobus sulfataricus gyrase-topoisomerase and
the T. thermophilus S14 C4 zinc-finger domains (Fig. 20.9). There is an identity of 14
out of 30 amino acids and a similarity of an additional 6 amino acids.
In conclusion, the S14 ribosomal protein from T. thermophilus has been
proven to bind Zn in a molar ratio of one. This and the absolute requirement of
the protein structure for the binding of Zn indicate that the C4 motif of TthS14
participates in the formation of a zinc-finger domain. Additional experiments are
needed to elucidate the role the domain might play in the interaction of the
TthS14 protein with rRNA and/or DNA.
7
Acknowledgements
This work was supported by a grant from the General Secretariat of Reserach and
Technology. The authors wish to thank the Laboratory of Analytical Chemistry of
the Chemistry Department for the atomic absorption measurements and Prof.
Ada Yonath for interest and support in this work.
References
Altschul SF, Gish W, Miller W, Myers EW & Lipman DJ (1990) Basic local alignment search tool. J Mol
BioI 215: 403-410
Archer TK, Hager GL & Omichinski JG (1990) Sequence-specific DNA binding by glucocorticoid
receptor "zinc-finger peptides". Proc Nat! Acad Sci USA 87: 7560-7564
Auer J, Spieker G & Boeck A (1989) Organization and structure of the Methanococcus transcriptional
unit homologous to the E. coli "spectinomycin operon". Implications for the evolutionary relationship oOOS and 80S ribosomes. J Mol Bioi 209: 21-28
Chan YL, Suzuki K, Olvera J & Wool IG (1993) Zinc-finger-like motifs in rat ribosomal proteins S27
and S29. Nucl Acids Res 21(3): 649-655
Choli, T. (1989) Structural properties of ribosomal protein L11 from Escerichia coli. Biochem. Int. 19,
l323-l338