Characterization of the domains of E. coli initiation factor IF2 responsible for recognition of the ribosome

We have studied the interactions between the ribosome and the domains of Escherichia coli translation initiation factor 2, using an in vitro ribosomal binding assay with wild-type forms, N- and C-terminal truncated forms of IF2 as well as isolated structural domains. A deletion mutant of the factor...

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Bibliographic Details
Published in:	FEBS letters Vol. 455; no. 1; pp. 130 - 134
Main Authors:	Moreno, Juan Manuel Palacios, Dyrskjøtersen, Lars, Kristensen, Janni Egebjerg, Mortensen, Kim Kusk, Sperling-Petersen, Hans Uffe
Format:	Journal Article
Language:	English
Published:	England Elsevier B.V 16-07-1999
Subjects:	Binding Sites Escherichia coli - metabolism IF1 IF2 IF3 In vitro ribosomal binding assay Models, Molecular Peptide Initiation Factors - chemistry Peptide Initiation Factors - metabolism Ribosomes - metabolism Sequence Deletion Translation initiation factor 2 In vitro ribosomal binding assay IF2 Translation initiation factor 2 IF1 IF3
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Summary:	We have studied the interactions between the ribosome and the domains of Escherichia coli translation initiation factor 2, using an in vitro ribosomal binding assay with wild-type forms, N- and C-terminal truncated forms of IF2 as well as isolated structural domains. A deletion mutant of the factor consisting of the two N-terminal domains of IF2, binds to both 30S and 50S ribosomal subunits as well as to 70S ribosomes. Furthermore, a truncated form of IF2, lacking the two N-terminal domains, binds to 30S ribosomal subunits in the presence of IF1. In addition, this N-terminal deletion mutant IF2 possess a low but significant affinity for the 70S ribosome which is increased by addition of IF1. The isolated C-terminal domain of IF2 has no intrinsic affinity for the ribosome nor does the deletion of this domain from IF2 affect the ribosomal binding capability of IF2. We conclude that the N-terminus of IF2 is required for optimal interaction of the factor with both 30S and 50S ribosomal subunits. A structural model for the interaction of IF2 with the ribosome is presented.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0014-5793 1873-3468
DOI:	10.1016/S0014-5793(99)00858-3