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

Katherine S Long; Bo T Porse

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

Katherine S Long, Bo T Porse

31 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	7
ISSN	0305-1048
Publication status	Published - 2003

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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.",

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

note = "Keywords: Anti-Bacterial Agents; Base Sequence; Binding Sites; Chloramphenicol; Escherichia coli; Halobacterium salinarum; Models, Molecular; Molecular Sequence Data; Nucleic Acid Conformation; Peptides; Protein Biosynthesis; RNA, Ribosomal, 23S; Ribonuclease H; Ribosomes; Ultraviolet Rays",

year = "2003",

language = "English",

volume = "31",

pages = "7208--15",

journal = "Nucleic Acids Research",

issn = "0305-1048",

publisher = "Oxford University Press",

number = "24",

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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

N1 - Keywords: Anti-Bacterial Agents; Base Sequence; Binding Sites; Chloramphenicol; Escherichia coli; Halobacterium salinarum; Models, Molecular; Molecular Sequence Data; Nucleic Acid Conformation; Peptides; Protein Biosynthesis; RNA, Ribosomal, 23S; Ribonuclease H; Ribosomes; Ultraviolet Rays

PY - 2003

Y1 - 2003

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.

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

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