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Gene Review:

TTHA1695 - elongation factor G

Thermus thermophilus HB8

Martemyanov, K.A. et al., Martemyanov, K.A. et al., Laurberg, M. et al., Hornung, V. et al., Hansson, S. et al., et al.

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Disease relevance of TTHA1695

Nucleotide sequence of the Thermus thermophilus HB8 gene coding for elongation factor G [1].
Here we present the crystal structures of two mutants of Thermus thermophilus EF-G, G16V and T84A, which exhibit FA hypersensitivity and resistance in vitro, respectively [2].

High impact information on TTHA1695

The crystal structure of Thermus thermophilus elongation factor G without guanine nucleotide was determined to 2.85 A [3].
Two hypersensitive and two resistant variants of elongation factor-G (EF-G) toward fusidic acid are studied in comparison with the wild type factor [4].
Two elongation factors (EF) EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome [5].
Domain III of elongation factor G from Thermus thermophilus is essential for induction of GTP hydrolysis on the ribosome [5].
The crystal structure of Thermus thermophilus elongation factor G (EF-G) carrying the point mutation His573Ala was determined at a resolution of 2.8 A [6].

Chemical compound and disease context of TTHA1695

Mutations in the G-domain of elongation factor G from Thermus thermophilus affect both its interaction with GTP and fusidic acid [4].

Biological context of TTHA1695

These results also suggest conformational changes of the EF-G molecule in the course of its interaction with the ribosome that might be induced by GTP binding and hydrolysis [5].
Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site [6].
The selected RNAs do not bind to elongation factor G. The EF-Tu binding RNAs share a short consensus sequence, 5'-ACCGAAG-3', which was also found in the alpha-sarcin domain of T. thermophilus23S rRNA [7].

Associations of TTHA1695 with chemical compounds

A correlation between fusidic acid resistance of EF-G mutants and their affinity to GTP are revealed in this study, although their interactions with GDP are not changed [4].

References

Nucleotide sequence of the Thermus thermophilus HB8 gene coding for elongation factor G. Yakhnin, A.V., Vorozheykina, D.P., Matvienko, N.I. Nucleic Acids Res. (1989) [Pubmed]
Structural insights into fusidic acid resistance and sensitivity in EF-G. Hansson, S., Singh, R., Gudkov, A.T., Liljas, A., Logan, D.T. J. Mol. Biol. (2005) [Pubmed]
Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. AEvarsson, A., Brazhnikov, E., Garber, M., Zheltonosova, J., Chirgadze, Y., al-Karadaghi, S., Svensson, L.A., Liljas, A. EMBO J. (1994) [Pubmed]
Mutations in the G-domain of elongation factor G from Thermus thermophilus affect both its interaction with GTP and fusidic acid. Martemyanov, K.A., Liljas, A., Yarunin, A.S., Gudkov, A.T. J. Biol. Chem. (2001) [Pubmed]
Domain III of elongation factor G from Thermus thermophilus is essential for induction of GTP hydrolysis on the ribosome. Martemyanov, K.A., Gudkov, A.T. J. Biol. Chem. (2000) [Pubmed]
Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. Laurberg, M., Kristensen, O., Martemyanov, K., Gudkov, A.T., Nagaev, I., Hughes, D., Liljas, A. J. Mol. Biol. (2000) [Pubmed]
In vitro selected RNA molecules that bind to elongation factor Tu. Hornung, V., Hofmann, H.P., Sprinzl, M. Biochemistry (1998) [Pubmed]

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