Structure-function relationship in Escherichia coli initiation factors. Identification of a lysine residue in the ribosomal binding site of initiation factor by site-specific chemical modification with pyridoxal phosphate.
Open Access
- 1 May 1981
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 256 (10) , 4905-4912
- https://doi.org/10.1016/s0021-9258(19)69342-7
Abstract
No abstract availableThis publication has 32 references indexed in Scilit:
- Structure-function relationship in Escherichia coli initiation factors: role of tyrosine residues in ribosomal binding and functional activity of IF-3Biochemistry, 1980
- Structure‐function relationships in Escherichia coliinitiation factorsFEBS Letters, 1979
- A novel Edman‐type degradation: direct formation of the thiohydantoin ring in alkaline solution by reaction of Edman‐type reagents with N‐monomethyl amino acidsFEBS Letters, 1978
- Separation of two forms of IF‐3 in Escherichia coli by two‐dimensional gel electrophoresisFEBS Letters, 1977
- Specific recognition of guanine bases in protein—nucleic acid complexesFEBS Letters, 1977
- Resistance of bacterial protein synthesis to double-stranded RNABiochemical and Biophysical Research Communications, 1974
- Active site-directed inhibition of E. coli DNA-dependent RNA polymerase by pyridoxal 5′-phosphateBiochemical and Biophysical Research Communications, 1973
- Nature of the ribosomal binding site for initiation factor 3 (IF-3)Biochemical and Biophysical Research Communications, 1973
- Purification and Properties of Initiation Factor F3Nature, 1970
- Réactions colorées spécifiques de l'arginine et de la tyrosine réalisées après chromatographie sur papierBiochimica et Biophysica Acta, 1952