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Mutational analysis of Glu272 in elongation factor 1A of E. coli.

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  • Klinisk Biokemisk Afdeling, SKS
  • Interdisciplinary Nanoscience Center
  • Molekylærbiologisk Institut
In our previous work (Mansilla et al. (1997) Protein Eng. 10, 927-934) we showed that Arg7 of Escherichia coli elongation factor Tu (EF1A) plays an essential role in aminoacyl-tRNA (aa-tRNA) binding. Substitution of Arg7 by Ala or Glu lost this activity. We proposed that Arg7 forms a salt bridge with the charged conserved amino acid Glu272 (Asp284 in Thermus aquaticus) thereby binding the N-terminal region of the protein to domain 2 and thus completing the conformational rearrangement needed for binding aa-tRNA. In this work we have mutated Glu272 to arginine, either alone (Glu272Arg), or in combination with one of the above mentioned mutations (Arg7Glu/Glu272Arg) in order to test this hypothesis. Our results show that, in confirmation of our thesis based on structural knowledge, the substitution of Glu272 (Asp284) decreases the ability of EF1A:GTP to bind aa-tRNA.
Udgivelsesdato: 1998-Jun-16
TidsskriftF E B S Letters
Sider (fra-til)417-20
Antal sider3
StatusUdgivet - 1998

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