[Ribosomal proteins directly interacting with fMet-tRNAfMet in the 30S initiation complex].
By means of ultraviolet-induced (254nm) RNA-protein cross-links it is shown, that tRNAfMet inside the preinitiation complex, formed by binding of fMet-tRNAfMet with 30S subunit of E. coli ribosome and RNA of the phage MS2 in the presence of initiation factors, directly interacts with proteins S4, S5, S9, S11, S14 and S15-S17.
D001426:Bacterial Proteins / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D010448:Peptide Initiation Factors / Q000378:metabolism*; D014176:Protein Biosynthesis; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D012358:RNA, Transfer, Met; D012269:Ribosomal Proteins / Q000378:metabolism*
D001426:Bacterial Proteins; D010448:Peptide Initiation Factors; D012346:RNA, Transfer, Amino Acyl; D012358:RNA, Transfer, Met; D012269:Ribosomal Proteins; C024988:tRNA, formylmethionine-
Ribosomnye belki, neposredstvenno vzaimodeĭstvuiushchie s fMet-tRNKfMet v 30S initsiatornom komplekse.