The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
Purification and characterization of Tet(M), a protein that renders ribosomes resistant to tetracycline.
Open accessAbstract
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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“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]
In the citing paper
“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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Metadata
- 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)
- 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
- 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
- Health Sciences › Medicine › Microbiology (medical) › 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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