For more than 50 years we have known antibiotics which target macromolecules in the elongation step of the translation machinery, in particular aminoglycosides. The initiation step however seems much more reluctant in providing us with efficient and specific inhibition targets for bacterial infections of humans.
It was recently discovered that two of the bacterial translation initiation factors, IF1 and IF2, are universal proteins found in homologous forms in all living organisms.
The presentation will concentrate on the bacterial IF2 (eIF5B in eukaryotes) and demonstrate characteristic "constant" and variable" regions in this protein. We have studied this factor in several bacteria and alignments of these in combination with databank sequence data of bIF2 from archae and eukaryotes reveals the C-terminal part to be conserved between different species while the N-terminal part is characteristic by its variability in both length and composition.
It is suggested that the species-specific N-terminal of IF2 may be useful as a target for species-specific selective drugs acting on the protein or the nucleic acid level.
In addition aspects of raising antibodies against the translation initiation factors, IF1 and IF2 will be discussed and results from immunochemical studies of these proteins will be presented.

□　連絡先：梅村　界渡（人間発達環境学研究科　蛯名研究室院生）
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