A conserved chloramphenicol binding site at the entrance to the ribosomal peptide exit tunnel

Katherine S Long; Bo T Porse

doi:10.1093/nar/gkg945

A conserved chloramphenicol binding site at the entrance to the ribosomal peptide exit tunnel

Katherine S Long, Bo T Porse

41 Citations (Scopus)

Abstract

The antibiotic chloramphenicol produces modifications in 23S rRNA when bound to ribosomes from the bacterium Escherichia coli and the archaeon Halobacterium halobium and irradiated with 365 nm light. The modifications map to nucleotides m(5)U747 and C2611/C2612, in domains II and V, respectively, of E.coli 23S rRNA and G2084 (2058 in E.coli numbering) in domain V of H.halobium 23S rRNA. The modification sites overlap with a portion of the macrolide binding site and cluster at the entrance to the peptide exit tunnel. The data correlate with the recently reported chloramphenicol binding site on an archaeal ribosome and suggest that a similar binding site is present on the E.coli ribosome.

Original language	English
Journal	Nucleic Acids Research
Volume	31
Issue number	24
Pages (from-to)	7208-15
Number of pages	8
ISSN	0305-1048
DOIs	https://doi.org/10.1093/nar/gkg945
Publication status	Published - 15 Dec 2003
Externally published	Yes

Keywords

Anti-Bacterial Agents/pharmacology
Base Sequence
Binding Sites
Chloramphenicol/metabolism
Escherichia coli/genetics
Halobacterium salinarum/genetics
Models, Molecular
Molecular Sequence Data
Nucleic Acid Conformation
Peptides/metabolism
Protein Biosynthesis
RNA, Ribosomal, 23S/chemistry
Ribonuclease H/metabolism
Ribosomes/drug effects
Ultraviolet Rays

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10.1093/nar/gkg945

Cite this

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title = "A conserved chloramphenicol binding site at the entrance to the ribosomal peptide exit tunnel",

abstract = "The antibiotic chloramphenicol produces modifications in 23S rRNA when bound to ribosomes from the bacterium Escherichia coli and the archaeon Halobacterium halobium and irradiated with 365 nm light. The modifications map to nucleotides m(5)U747 and C2611/C2612, in domains II and V, respectively, of E.coli 23S rRNA and G2084 (2058 in E.coli numbering) in domain V of H.halobium 23S rRNA. The modification sites overlap with a portion of the macrolide binding site and cluster at the entrance to the peptide exit tunnel. The data correlate with the recently reported chloramphenicol binding site on an archaeal ribosome and suggest that a similar binding site is present on the E.coli ribosome.",

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author = "Long, {Katherine S} and Porse, {Bo T}",

year = "2003",

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doi = "10.1093/nar/gkg945",

language = "English",

volume = "31",

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journal = "Nucleic Acids Research",

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TY - JOUR

T1 - A conserved chloramphenicol binding site at the entrance to the ribosomal peptide exit tunnel

AU - Long, Katherine S

AU - Porse, Bo T

PY - 2003/12/15

Y1 - 2003/12/15

N2 - The antibiotic chloramphenicol produces modifications in 23S rRNA when bound to ribosomes from the bacterium Escherichia coli and the archaeon Halobacterium halobium and irradiated with 365 nm light. The modifications map to nucleotides m(5)U747 and C2611/C2612, in domains II and V, respectively, of E.coli 23S rRNA and G2084 (2058 in E.coli numbering) in domain V of H.halobium 23S rRNA. The modification sites overlap with a portion of the macrolide binding site and cluster at the entrance to the peptide exit tunnel. The data correlate with the recently reported chloramphenicol binding site on an archaeal ribosome and suggest that a similar binding site is present on the E.coli ribosome.

AB - The antibiotic chloramphenicol produces modifications in 23S rRNA when bound to ribosomes from the bacterium Escherichia coli and the archaeon Halobacterium halobium and irradiated with 365 nm light. The modifications map to nucleotides m(5)U747 and C2611/C2612, in domains II and V, respectively, of E.coli 23S rRNA and G2084 (2058 in E.coli numbering) in domain V of H.halobium 23S rRNA. The modification sites overlap with a portion of the macrolide binding site and cluster at the entrance to the peptide exit tunnel. The data correlate with the recently reported chloramphenicol binding site on an archaeal ribosome and suggest that a similar binding site is present on the E.coli ribosome.

KW - Anti-Bacterial Agents/pharmacology

KW - Base Sequence

KW - Binding Sites

KW - Chloramphenicol/metabolism

KW - Escherichia coli/genetics

KW - Halobacterium salinarum/genetics

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Nucleic Acid Conformation

KW - Peptides/metabolism

KW - Protein Biosynthesis

KW - RNA, Ribosomal, 23S/chemistry

KW - Ribonuclease H/metabolism

KW - Ribosomes/drug effects

KW - Ultraviolet Rays

U2 - 10.1093/nar/gkg945

DO - 10.1093/nar/gkg945

M3 - Journal article

C2 - 14654696

SN - 0305-1048

VL - 31

SP - 7208

EP - 7215

JO - Nucleic Acids Research

JF - Nucleic Acids Research

IS - 24

ER -

A conserved chloramphenicol binding site at the entrance to the ribosomal peptide exit tunnel

Abstract

Keywords

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