Functional implication of the sole arginine residue of ribosomal proteins L7/L12
Author:
Publisher
Springer Science and Business Media LLC
Subject
Genetics,Molecular Biology,General Medicine
Link
http://link.springer.com/content/pdf/10.1007/BF00776977.pdf
Reference18 articles.
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2. CampuzanoS., VázquezD. & ModolellJ., 1979. Dissociation of guanosine nucleotide-elongation factor G-ribosome complexes. Biochemistry 18: 1570?1574.
3. GudkovA. T. & BehlkeJ., 1978. The N-terminal sequence protein of L7/L12 is responsible for its dimerization. Eur. J. Biochem. 90: 309?312.
4. HamelE., KokaM. & NakamotoT., 1972. Requirement of an Escherichia coli 50S ribosomal protein component for effective interaction of the ribosome with T and G factors and with guanosine triphosphate. J. Biol. Chem. 247: 805?814.
5. HernándezF., López-RivasA., Pintor-ToroJ. A. & PalaciánE., 1982. Implication of arginyl residues in aminoacyl-tRNA binding to ribosomes. Eur. J. Biochem. 123: 95?98.
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1. Control of phosphate release from elongation factor G by ribosomal protein L7/12;The EMBO Journal;2005-11-17
2. Interaction of Helix D of Elongation Factor Tu with Helices 4 and 5 of Protein L7/12 on the Ribosome;Journal of Molecular Biology;2004-03
3. Structure and Function of the Acidic Ribosomal Stalk Proteins;Current Protein and Peptide Science;2002-02-01
4. A Common Structural Motif in Elongation Factor Ts and Ribosomal Protein L7/12 May Be Involved in the Interaction with Elongation Factor Tu;Journal of Molecular Evolution;2001-02
5. Structure–Function Relationships in the Ribosomal Protein L12 in the ArchaeonSulfolobus acidocaldarius;Archives of Biochemistry and Biophysics;1999-05
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