[Ribosomal proteins interacting with Phe-tRNAPhe during enzymatic binding with translating ribosome before and after the release of the elongation factor EF-Tu].
Proteins, directly interacting with tRNA in R- and A-sites of E. coli ribosome were determined by means of ultraviolet-induced RNA-protein cross-links. It is shown, that tRNAPhe in the R-site (upon enzymatic binding of the ternary complex Phe-tRNAPhe. X Tu X GMPPCP to ribosome) directly interact with factor Tu and ribosomal proteins S4, S5, S8 and L6, while in the A-site (upon binding of Phe-tRNAPhe X Tu X GTP, GTP hydrolysis, Tu release and transpeptidation)--with proteins S5, S10, L6, L16 and S13/S14/L27.
D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D010444:Peptide Elongation Factor Tu; D010445:Peptide Elongation Factors / Q000235:genetics / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000235:genetics* / Q000378:metabolism; D012269:Ribosomal Proteins / Q000235:genetics / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*; D014466:Ultraviolet Rays
D010445:Peptide Elongation Factors; D012346:RNA, Transfer, Amino Acyl; D012269:Ribosomal Proteins; C037801:tRNA, phenylalanylphenylalanine-; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu
Ribosomnye belki, vzaimodeĭstvuiushchie s Phe-tRNKPhe pri énzimaticheskom sviazyvanii s transliruiushcheĭ ribosomoĭ do i posle ukhoda faktora élongatsii EF-Tu.