Determination of tRNA nucleotide residues directly interacting with proteins in the post- and pretranslocated ribosomal complexes.
Nucleotide residues of E. coli tRNA interacting directly with proteins in pre- and posttranslocated ribosomal complexes have been identified by analysis of photo-induced tRNA-protein cross-links. A9, G18, A26 and U59 residues of NAcPhePhe-tRNA, located in the Ab-site (pretranslocated complex) have been cross-linked with proteins S10, L27, S7 and L2 respectively. In deacylated tRNA, located in the Pb-site, residues C17, G44, C56 and U60 have been cross-linked with proteins L2, L5, L27 and S9 respectively. The G44-L5 cross-link disappeared after translocation (NAc-PhePhe-tRNA located in the Pt-site).
Zelinsky Institute of Organic Chemistry, USSR Academy of Sciences, Moscow.
G G
GG
Abdurashidova
E A
EA
Tsvetkova
E I
EI
Budowsky
D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D008961:Models, Structural; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D012323:RNA Processing, Post-Transcriptional; D012343:RNA, Transfer / Q000235:genetics / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism*
D012269:Ribosomal Proteins; D012343:RNA, Transfer