E. colitranslation initiation factor IF2 – an extremely conserved protein. Comparative sequence analysis of the infBgene in clinical isolates of E. coli

Autor: de A. Steffensen, Søren A, Poulsen, Ane B, Mortensen, Kim K, Sperling-Petersen, Hans U
Zdroj: FEBS Letters; December 1997, Vol. 419 Issue: 2-3 p281-284, 4p
Abstrakt: The functionally uncharacterised N‐terminal of translation initiation factor IF2 has been found to be extremely variable when comparing different bacterial species. In order to study the intraspecies variability of IF2 the 2670 basepairs nucleotide sequence of the infBgene (encoding IF2) was determined in 10 clinical isolates of E. coli. The N‐terminal domains (I, II and III) were completely conserved indicating a specific function of this region of IF2. Only one polymorphic position was found in the deduced 890 amino acid sequence. This Gln/Gly490 is located within the central GTP/GDP‐binding domain IV of IF2. The results are further evidence that IF2 from E. colihas reached a highly defined level of structural and functional development.
Databáze: Supplemental Index