The N-terminal half of initiation factor IF3 is folded as a stable independent domain
- 31 December 1994
- Vol. 76 (5) , 376-383
- https://doi.org/10.1016/0300-9084(94)90111-2
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- Structure-function analysis of Escherichia coli translation initiation factor IF3: tyrosine 107 and lysine 110 are required for ribosome bindingBiochemistry, 1992
- Domains of initiator tRNA and initiation codon crucial for initiator tRNA selection by Escherichia coli IF3.Genes & Development, 1990
- Selection of the initiator tRNA by Escherichia coli initiation factors.Genes & Development, 1989
- Genetic engineering of methionyl-tRNA synthetase: in vitro regeneration of an active synthetase by proteolytic cleavage of a methionyl-tRNA synthetase-β-galactosidase chimeric proteinBiochimie, 1988
- Analytical strategy for determination of active site sequences in aminoacyl-tRNA synthetasesJournal of Chromatography A, 1988
- The unusual translational initiation codon AUU limits the expression of the infC (initiation factor IF3) gene of Escherichia coliMolecular Genetics and Genomics, 1987
- Escherichia coli protein synthesis initiation factor IF3 controls its own gene expression at the translational level in vivoJournal of Molecular Biology, 1986
- Cross-linking of initiation factor IF3 toEscherichia coli30S ribosomal subunit by trans-dlamminedichloroplatinum(II): characterization of two cross-linking sites in 16S rRNA; a possible way of functioning for IF3Nucleic Acids Research, 1986
- Nuclease mapping of the secondary structure of the 49-nucleotide 3' terminal cloacin fragment ofEscherichia coli16S RNA and its interactions with initiation factor 3Nucleic Acids Research, 1983
- Initiation Factors in Protein BiosynthesisAnnual Review of Biochemistry, 1982