[Proteins contacting with peptidyl-tRNA at the A-site of the Escherichia coli ribosome after enzymatic and non-enzymatic binding of aminoacyl-tRNA].
Proteins contacting (directly interacting) with peptidyl-tRNA in the A-site of E. coli ribosome were determined by means of ultraviolet-induced RNA-protein cross-linking. It has been shown that upon enzymatic binding of Phe-tRNAPhe with the posttranslocated ribosome and following transpeptidation, the peptidyl-tRNAPhe directly interacts with proteins S5, S10, L6, L16 and S13/S14/L27, while upon non-enzymatic binding--with S5, S10, L2, L6 and L16. These data evidenced, that the difference in tRNA-protein interactions upon enzymatic and non-enzymatic binding of Phe-tRNAPhe to the ribosome does not prevent the following step and remains after transpeptidation.
G G
GG
Abdurashidova
V A
VA
Ovsepian
E I
EI
Budovskiĭ
D004926:Escherichia coli / Q000378:metabolism*; D014176:Protein Biosynthesis; D012329:RNA, Bacterial / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*
D012329:RNA, Bacterial; D012346:RNA, Transfer, Amino Acyl; D012269:Ribosomal Proteins
Belki, kontaktiruiushchie s peptidil-tRNK v A-uchastke ribosomy Escherichia coli posle énzimaticheskogo i neénzimaticheskogo sviazyvaniia aminoatsil-tRNK.