Movement of the 3'-end of tRNA through the peptidyl transferase centre and its inhibition by antibiotics

TY - JOUR

T1 - Movement of the 3'-end of tRNA through the peptidyl transferase centre and its inhibition by antibiotics

AU - Kirillov, Stanislav

AU - Porse, Bo Torben

AU - Vester, Birthe

AU - Woolley, Paul

AU - Garrett, Roger Antony

N1 - Keywords: Anti-Bacterial Agents; Base Sequence; Binding Sites; Molecular Sequence Data; Nucleic Acid Conformation; Peptides; Peptidyl Transferases; RNA, Bacterial; RNA, Transfer; RNA, Transfer, Amino Acyl; Ribosomes

PY - 1997

Y1 - 1997

N2 - Determining how antibiotics inhibit ribosomal activity requires a detailed understanding of the interactions and relative movement of tRNA, mRNA and the ribosome. Recent models for the formation of hybrid tRNA binding sites during the elongation cycle have provided a basis for re-evaluating earlier experimental data and, especially, those relevant to substrate movements through the peptidyl transferase centre. With the exception of deacylated tRNA, which binds at the E-site, ribosomal interactions of the 3'-ends of the tRNA substrates generate only a small part of the total free energy of tRNA-ribosome binding. Nevertheless, these relatively weak interactions determine the unidirectional movement of tRNAs through the ribosome and, moreover, they appear to be particularly susceptible to perturbation by antibiotics. Here we summarise current ideas relating particularly to the movement of the 3'-ends of tRNA through the ribosome and consider possible inhibitory mechanisms of the peptidyl transferase antibiotics.

AB - Determining how antibiotics inhibit ribosomal activity requires a detailed understanding of the interactions and relative movement of tRNA, mRNA and the ribosome. Recent models for the formation of hybrid tRNA binding sites during the elongation cycle have provided a basis for re-evaluating earlier experimental data and, especially, those relevant to substrate movements through the peptidyl transferase centre. With the exception of deacylated tRNA, which binds at the E-site, ribosomal interactions of the 3'-ends of the tRNA substrates generate only a small part of the total free energy of tRNA-ribosome binding. Nevertheless, these relatively weak interactions determine the unidirectional movement of tRNAs through the ribosome and, moreover, they appear to be particularly susceptible to perturbation by antibiotics. Here we summarise current ideas relating particularly to the movement of the 3'-ends of tRNA through the ribosome and consider possible inhibitory mechanisms of the peptidyl transferase antibiotics.

M3 - Journal article

C2 - 9136892

SN - 0014-5793

VL - 406

SP - 223

EP - 233

JO - F E B S Letters

JF - F E B S Letters

IS - 3

ER -