Nucleotide residues of tRNA, directly interacting with proteins within the complex of the 30 S subunit of E. coli ribosome with poly(U) and NAcPhe-tRNA(Phe).
With the aid of photoinduced tRNA-protein cross-linking, nucleotide residues A21, U45 and U60 were shown to interact directly with proteins S5, S7 and S9 respectively, in the complex of the 30 S subunit of E. coli ribosome with poly(U) and NAcPhe-tRNA(Phe). These nucleotide residues are located in the central part of the L-form in the tertiary structure of RNA.
Abdurashidova
G G
GG
Zelinsky Institute of Organic Chemistry, USSR Academy of Sciences, Moscow.
Tsvetkova
E A
EA
Budowsky
E I
EI
D001426:Bacterial Proteins / Q000378:metabolism; D001665:Binding Sites; D004926:Escherichia coli / Q000378:metabolism*; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011072:Poly U / Q000378:metabolism* / Q000528:radiation effects; D011485:Protein Binding; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism* / Q000528:radiation effects; D012265:Ribonucleotides / Q000378:metabolism; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*; D014466:Ultraviolet Rays
D001426:Bacterial Proteins; D012346:RNA, Transfer, Amino Acyl; D012265:Ribonucleotides; D012269:Ribosomal Proteins; C006383:tRNA, N-acetylphenylalanine-; D011072:Poly U