Purification and characterization of Tet(M), a protein that renders ribosomes resistant to tetracycline.

Burdett, V

doi:10.1016/s0021-9258(18)49928-0

Cited by 141RNA and protein synthesis mechanismsAntibiotic Resistance in BacteriaBacterial Genetics and Biotechnology

Purification and characterization of Tet(M), a protein that renders ribosomes resistant to tetracycline.

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Burdett, V·1991·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(18)49928-0

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Abstract

The tet(M) tetracycline resistance gene has been found in a wide variety of clinically important bacteria. It has been shown previously (Burdett, V. (1986) J. Bacteriol. 165, 564-569) that the tet(M) gene product mediates resistance at the level of protein synthesis as judged by in vitro assay. Using this assay, large amounts of protein were purified from an Escherichia coli overproducer expressing the gene under control of a T7 promoter. The purified activity consists of a single polypeptide of molecular weight 68,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and was confirmed to be the tet(M) gene product by amino-terminal sequence analysis. Purified Tet(M) has an associated ribosome-dependent GTPase with the specific activity being similar to that of the corresponding activity associated with elongation factor G. Since Tet(M) also displays substantial homology to elongation factor G throughout its length, Tet(M) may function as an analog of this elongation factor.

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RPPs bind and hydrolyze GTP in a ribosome-dependent manner, and maintenance of this activity is important for in vivo activity.
“Accordingly, the RPPs bind and hydrolyze GTP in a ribosome-dependent manner (5, 6, 53), and maintenance of this activity is important for in vivo activity (11, 23).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [5]
Tet(M) cannot substitute for the elongation factors in vivo or in vitro.
“however, Burdett (5, 6) showed that Tet(M) cannot substitute for the elongation factors in vivo or in vitro.”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [5]

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Tet(M)-promoted release of tetracycline from ribosomes is GTP dependent
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Ribosomal Protection from Tetracycline Mediated by Tet(O): Tet(O) Interaction with Ribosomes Is GTP-Dependent
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Binding Interaction between Tet(M) and the Ribosome: Requirements for Binding
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Localization of the Ribosomal Protection Protein Tet(O) on the Ribosome and the Mechanism of Tetracycline Resistance
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Authors: Burdett, V
Affiliations: Duke Medical Center (US)
Corresponding author: Burdett, V
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1991-02
Volume: 266
Issue: 5
Pages: 2872-2877
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(18)49928-0
OpenAlex: W1537838130
Cited by: 141
References: 39
Citations by year: 2026: 2 · 2025: 2 · 2024: 1 · 2023: 2 · 2022: 4 · 2021: 3 · 2020: 5 · 2019: 2 · 2018: 2 · 2017: 5 · 2016: 3 · 2015: 6 · 2014: 6 · 2013: 4 · 2012: 5
FWCI: 2.91
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 10844 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01ai015619-18)
National Institute of Allergy and Infectious Diseases (AI15619)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Medicine › Antibiotic Resistance in Bacteria
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords: tetM, tetracycline resistance, ribosome protection, ribosome-associated GTPase, protein synthesis inhibition, T7 promoter, N-terminal sequence, antibiotic resistance mechanisms
MeSH terms: Amino Acid Sequence, Amino Acids, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Genes, Bacterial, Hot Temperature, Hydrolysis, Molecular Sequence Data, Mutation, Peptide Elongation Factor Tu, Peptide Elongation Factors, Plasmids, Repressor Proteins, Ribosomes, Sequence Homology, Nucleic Acid, Tetracycline Resistance, Peptide Elongation Factor G, GTP Phosphohydrolase-Linked Elongation Factors

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Purification and characterization of Tet(M), a protein that renders ribosomes resistant to tetracycline.

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