Dependence of Initiation Factor IF-2 Activity on Proteins L7 and L12 from Escherichia coli 50 S Ribosomes
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference30 articles.
1. The interrelationship between guanosine triphosphatase and amino acid polymerization
2. Peptide Chain Elongation: GTP Cleavage catalysed by Factors binding Aminoacyl-Transfer RNA to the Ribosome
3. Guanosine 5'-triphosphatase activity of initiation factor f2.
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5. Studies on the Role of an Escherichia coli 50 S Ribosomal Component in Polypeptide Chain Elongation
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1. Asymmetric Interactions between the Acidic P1 and P2 Proteins in the Saccharomyces cerevisiae Ribosomal Stalk;Journal of Biological Chemistry;2001-08
2. Characterization of the domains ofE. coliinitiation factor IF2 responsible for recognition of the ribosome;FEBS Letters;1999-07-15
3. Structure–Function Relationships in the Ribosomal Protein L12 in the ArchaeonSulfolobus acidocaldarius;Archives of Biochemistry and Biophysics;1999-05
4. The L7/L12 ribosomal domain of the ribosome: structural and functional studies;FEBS Letters;1997-05-05
5. An inhibitor of elongation factor G (EF-G) GTPase present in the ribosome wash of Escherichia coli: a complex of initiation factors IF1 and IF3?;Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression;1992-01
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