Macromolecular mimicry in translation initiation: a model for the initiation factor IF2 on the ribosome.
Protein biosynthesis in bacteria is controlled by a number of translation factors. Recent data based on comparison of sequence and structure data of translation factors have established a novel hypothesis for their interaction with the ribosome: initiation, elongation, and termination factors may use a common or partly overlapping binding site on the ribosome in a process of macromolecular mimicry of an A-site-bound tRNA. This paper reviews structural knowledge and tRNA macromolecular mimicry involvement of translation initiation factor IF2. Furthermore, a model is proposed for the factor and its interaction with the ribosome during the formation of the translation initiation complex.
Moreno
J M
JM
Department of Molecular and Structural Biology, Aarhus University, Denmark.
Sørensen
H P
HP
Mortensen
K K
KK
Sperling-Petersen
H U
HU
D015977:Eukaryotic Initiation Factor-1 / Q000737:chemistry / Q000378:metabolism; D018716:Molecular Mimicry; D010448:Peptide Initiation Factors / Q000737:chemistry* / Q000378:metabolism*; D039881:Prokaryotic Initiation Factor-2; D014176:Protein Biosynthesis; D012343:RNA, Transfer / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism*
D015977:Eukaryotic Initiation Factor-1; D010448:Peptide Initiation Factors; D039881:Prokaryotic Initiation Factor-2; D012343:RNA, Transfer