Antibiotic inhibition of the movement of tRNA substrates through a peptidyl transferase cavity.

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Antibiotic inhibition of the movement of tRNA substrates through a peptidyl transferase cavity. / Porse, B T; Rodriguez-Fonseca, C; Leviev, I; Garrett, R A.

In: Biochemistry and Cell Biology, Vol. 73, No. 11-12, 1996, p. 877-85.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Porse, BT, Rodriguez-Fonseca, C, Leviev, I & Garrett, RA 1996, 'Antibiotic inhibition of the movement of tRNA substrates through a peptidyl transferase cavity.', Biochemistry and Cell Biology, vol. 73, no. 11-12, pp. 877-85.

APA

Porse, B. T., Rodriguez-Fonseca, C., Leviev, I., & Garrett, R. A. (1996). Antibiotic inhibition of the movement of tRNA substrates through a peptidyl transferase cavity. Biochemistry and Cell Biology, 73(11-12), 877-85.

Vancouver

Porse BT, Rodriguez-Fonseca C, Leviev I, Garrett RA. Antibiotic inhibition of the movement of tRNA substrates through a peptidyl transferase cavity. Biochemistry and Cell Biology. 1996;73(11-12):877-85.

Author

Porse, B T ; Rodriguez-Fonseca, C ; Leviev, I ; Garrett, R A. / Antibiotic inhibition of the movement of tRNA substrates through a peptidyl transferase cavity. In: Biochemistry and Cell Biology. 1996 ; Vol. 73, No. 11-12. pp. 877-85.

Bibtex

@article{955b11f058a311dd8d9f000ea68e967b,
title = "Antibiotic inhibition of the movement of tRNA substrates through a peptidyl transferase cavity.",
abstract = "The present review attempts to deal with movement of tRNA substrates through the peptidyl transferase centre on the large ribosomal subunit and to explain how this movement is interrupted by antibiotics. It builds on the concept of hybrid tRNA states forming on ribosomes and on the observed movement of the 5' end of P-site-bound tRNA relative to the ribosome that occurs on peptide bond formation. The 3' ends of the tRNAs enter, and move through, a catalytic cavity where antibiotics are considered to act by at least three primary mechanisms: (i) they interfere with the entry of the aminoacyl moiety into the catalytic cavity before peptide bond formation; (ii) they inhibit movement of the nascent peptide along the peptide channel, a process that may generally involve destabilization of the peptidyl tRNA, and (iii) they prevent movement of the newly deacylated tRNA between the P/P and hybrid P/E sites on peptide bond formation.",
author = "Porse, {B T} and C Rodriguez-Fonseca and I Leviev and Garrett, {R A}",
note = "Keywords: Anti-Bacterial Agents; Base Sequence; Binding Sites; Catalysis; Molecular Sequence Data; Motion; Nucleic Acid Conformation; Peptidyl Transferases; RNA, Transfer",
year = "1996",
language = "English",
volume = "73",
pages = "877--85",
journal = "Biochemistry and Cell Biology",
issn = "0829-8211",
publisher = "N R C Research Press",
number = "11-12",

}

RIS

TY - JOUR

T1 - Antibiotic inhibition of the movement of tRNA substrates through a peptidyl transferase cavity.

AU - Porse, B T

AU - Rodriguez-Fonseca, C

AU - Leviev, I

AU - Garrett, R A

N1 - Keywords: Anti-Bacterial Agents; Base Sequence; Binding Sites; Catalysis; Molecular Sequence Data; Motion; Nucleic Acid Conformation; Peptidyl Transferases; RNA, Transfer

PY - 1996

Y1 - 1996

N2 - The present review attempts to deal with movement of tRNA substrates through the peptidyl transferase centre on the large ribosomal subunit and to explain how this movement is interrupted by antibiotics. It builds on the concept of hybrid tRNA states forming on ribosomes and on the observed movement of the 5' end of P-site-bound tRNA relative to the ribosome that occurs on peptide bond formation. The 3' ends of the tRNAs enter, and move through, a catalytic cavity where antibiotics are considered to act by at least three primary mechanisms: (i) they interfere with the entry of the aminoacyl moiety into the catalytic cavity before peptide bond formation; (ii) they inhibit movement of the nascent peptide along the peptide channel, a process that may generally involve destabilization of the peptidyl tRNA, and (iii) they prevent movement of the newly deacylated tRNA between the P/P and hybrid P/E sites on peptide bond formation.

AB - The present review attempts to deal with movement of tRNA substrates through the peptidyl transferase centre on the large ribosomal subunit and to explain how this movement is interrupted by antibiotics. It builds on the concept of hybrid tRNA states forming on ribosomes and on the observed movement of the 5' end of P-site-bound tRNA relative to the ribosome that occurs on peptide bond formation. The 3' ends of the tRNAs enter, and move through, a catalytic cavity where antibiotics are considered to act by at least three primary mechanisms: (i) they interfere with the entry of the aminoacyl moiety into the catalytic cavity before peptide bond formation; (ii) they inhibit movement of the nascent peptide along the peptide channel, a process that may generally involve destabilization of the peptidyl tRNA, and (iii) they prevent movement of the newly deacylated tRNA between the P/P and hybrid P/E sites on peptide bond formation.

M3 - Journal article

C2 - 8722003

VL - 73

SP - 877

EP - 885

JO - Biochemistry and Cell Biology

JF - Biochemistry and Cell Biology

SN - 0829-8211

IS - 11-12

ER -

ID: 5142431