Tet(O), a protein that mediates ribosomal protection to tetracycline, binds, and hydrolyses GTP

1995 ◽  
Vol 41 (11) ◽  
pp. 965-970 ◽  
Author(s):  
Diane E. Taylor ◽  
Lori J. Jerome ◽  
Jaswinder Grewal ◽  
Nicholas Chang
Keyword(s):  
G Proteins ◽  
Campylobacter Jejuni ◽  
Binding Assay ◽  
Tetracycline Resistance ◽  
Carboxyl Terminus ◽  
Tetracycline Resistance Gene ◽  
Gtp Hydrolysis ◽  
Amino Terminal ◽  
Ribosomal Protection ◽  
Hydrolysis Activity

The tet(O) tetracycline resistance gene, originally cloned from Campylobacter jejuni, mediates resistance by ribosomal protection. Using partially purified Tet(O) protein of 68 000 Da whose identity was verified by ribosomal protection assays, amino terminal sequencing, and immunoblotting using an antibody raised against the deduced 15 amino acids at the carboxyl terminus of the Tet(O) protein, the Tet(O) protein was found to bind to [α-32P]GTP and [3H]GDP using a filter binding assay. [γ-32P]GTP hydrolysis by Tet(O) was also demonstrated and was found to be time dependent with more than 50% of the hydrolysis activity occurring within the first 5 min. The GTPase activity of Tet(O) appears to be ribosome dependent, suggesting that ribosomes act as an effector similar to other G proteins involved in signal transduction.Key words: ribosomes, tetracycline resistance, GTPase, protein synthesis.

Nucleotide sequence analysis and expression of a tetracycline-resistance gene from Campylobacter jejuni

Gene ◽  
1988 ◽  
Vol 62 (1) ◽  
pp. 17-26 ◽  
Author(s):  
Elias K. Manavathu ◽  
Koji Hiratsuka ◽  
Diane E. Taylor
Keyword(s):  
Sequence Analysis ◽  
Nucleotide Sequence ◽  
Resistance Gene ◽  
Campylobacter Jejuni ◽  
Tetracycline Resistance ◽  
Nucleotide Sequence Analysis ◽  
Tetracycline Resistance Gene

scholarly journals Identification of the tetracycline resistance gene, tet(O), in Streptococcus pneumoniae.

1996 ◽  
Vol 40 (12) ◽  
pp. 2891-2893 ◽  
Author(s):  
C A Widdowson ◽  
K P Klugman ◽  
D Hanslo
Keyword(s):  
Streptococcus Pneumoniae ◽  
Resistance Gene ◽  
Campylobacter Jejuni ◽  
Nucleotide Sequence Identity ◽  
Amino Acid Sequence Identity ◽  
Tetracycline Resistance ◽  
Campylobacter Coli ◽  
Tetracycline Resistance Gene ◽  
Sequence Identity ◽  
First Time

Five isolates of Streptococcus pneumoniae resistant to tetracycline but lacking tet(M) were studied. The tetracycline resistance gene, tet(O), was detected for the first time in the pneumococcus. The gene was amplified and sequenced and found to share 99% nucleotide sequence identity and 99, 99, and 98% deduced amino acid sequence identity with the tet(O) resistance genes of Streptococcus mutans, Campylobacter coli, and Campylobacter jejuni, respectively.

scholarly journals Characterization and expression of a cloned tetracycline resistance determinant from Campylobacter jejuni plasmid pUA466.

1987 ◽  
Vol 169 (7) ◽  
pp. 2984-2989 ◽  
Author(s):  
D E Taylor ◽  
K Hiratsuka ◽  
H Ray ◽  
E K Manavathu
Keyword(s):  
Campylobacter Jejuni ◽  
Tetracycline Resistance ◽  
Resistance Determinant

scholarly journals Tetracycline resistance of Australian Campylobacter jejuni and Campylobacter coli isolates

2005 ◽  
Vol 55 (4) ◽  
pp. 452-460 ◽  
Author(s):  
A. Pratt ◽  
V. Korolik
Keyword(s):  
Campylobacter Jejuni ◽  
Tetracycline Resistance ◽  
Campylobacter Coli

scholarly journals In Vitro and In Vivo Antibacterial Activities of a Novel Glycylcycline, the 9-t-Butylglycylamido Derivative of Minocycline (GAR-936)

1999 ◽  
Vol 43 (4) ◽  
pp. 738-744 ◽  
Author(s):  
P. J. Petersen ◽  
N. V. Jacobus ◽  
W. J. Weiss ◽  
P. E. Sum ◽  
R. T. Testa
Keyword(s):  
Anaerobic Bacteria ◽  
Tetracycline Resistance ◽  
Protective Effects ◽  
Gram Negative ◽  
E Coli ◽  
Resistance Determinants ◽  
Aerobic And Anaerobic ◽  
Ribosomal Protection

ABSTRACT The 9-t-butylglycylamido derivative of minocycline (TBG-MINO) is a recently synthesized member of a novel group of antibiotics, the glycylcyclines. This new derivative, like the first glycylcyclines, theN,N-dimethylglycylamido derivative of minocycline and 6-demethyl-6-deoxytetracycline, possesses activity against bacterial isolates containing the two major determinants responsible for tetracycline resistance: ribosomal protection and active efflux. The in vitro activities of TBG-MINO and the comparative agents were evaluated against strains with characterized tetracycline resistance as well as a spectrum of recent clinical aerobic and anaerobic gram-positive and gram-negative bacteria. TBG-MINO, with an MIC range of 0.25 to 0.5 μg/ml, showed good activity against strains expressing tet(M) (ribosomal protection), tet(A), tet(B),tet(C), tet(D), and tet(K) (efflux resistance determinants). TBG-MINO exhibited similar activity against methicillin-resistant Staphylococcus aureus (MRSA), penicillin-resistant streptococci, and vancomycin-resistant enterococci (MICs at which 90% of strains are inhibited, ≤0.5 μg/ml). TBG-MINO exhibited activity against a wide diversity of gram-negative aerobic and anaerobic bacteria, most of which were less susceptible to tetracycline and minocycline. The in vivo protective effects of TBG-MINO were examined against acute lethal infections in mice caused by Escherichia coli, S. aureus, andStreptococcus pneumoniae isolates. TBG-MINO, administered intravenously, demonstrated efficacy against infections caused byS. aureus including MRSA strains and strains containingtet(K) or tet(M) resistance determinants (median effective doses [ED50s], 0.79 to 2.3 mg/kg of body weight). TBG-MINO demonstrated efficacy against infections caused by tetracycline-sensitive E. coli strains as well asE. coli strains containing either tet(M) or the efflux determinant tet(A), tet(B), ortet(C) (ED50s, 1.5 to 3.5 mg/kg). Overall, TBG-MINO shows antibacterial activity against a wide spectrum of gram-positive and gram-negative aerobic and anaerobic bacteria including strains resistant to other chemotherapeutic agents. The in vivo protective effects, especially against infections caused by resistant bacteria, corresponded with the in vitro activity of TBG-MINO.

scholarly journals FlhF and Its GTPase Activity Are Required for Distinct Processes in Flagellar Gene Regulation and Biosynthesis in Campylobacter jejuni

2009 ◽  
Vol 191 (21) ◽  
pp. 6602-6611 ◽  
Author(s):  
Murat Balaban ◽  
Stephanie N. Joslin ◽  
David R. Hendrixson
Keyword(s):  
Gene Expression ◽  
Gene Regulation ◽  
Campylobacter Jejuni ◽  
Regulatory System ◽  
Flagellar Gene ◽  
Gtpase Activity ◽  
Gtp Hydrolysis ◽  
Genetic Analyses ◽  
Flagellar Biosynthesis ◽  
Two Component

ABSTRACT FlhF proteins are putative GTPases that are often necessary for one or more steps in flagellar organelle development in polarly flagellated bacteria. In Campylobacter jejuni, FlhF is required for σ54-dependent flagellar gene expression and flagellar biosynthesis, but how FlhF influences these processes is unknown. Furthermore, the GTPase activity of any FlhF protein and the requirement of this speculated activity for steps in flagellar biosynthesis remain uncharacterized. We show here that C. jejuni FlhF hydrolyzes GTP, indicating that these proteins are GTPases. C. jejuni mutants producing FlhF proteins with reduced GTPase activity were not severely defective for σ54-dependent flagellar gene expression, unlike a mutant lacking FlhF. Instead, these mutants had a propensity to lack flagella or produce flagella in improper numbers or at nonpolar locations, indicating that GTP hydrolysis by FlhF is required for proper flagellar biosynthesis. Additional studies focused on elucidating a possible role for FlhF in σ54-dependent flagellar gene expression were conducted. These studies revealed that FlhF does not influence production of or signaling between the flagellar export apparatus and the FlgSR two-component regulatory system to activate σ54. Instead, our data suggest that FlhF functions in an independent pathway that converges with or works downstream of the flagellar export apparatus-FlgSR pathway to influence σ54-dependent gene expression. This study provides corroborative biochemical and genetic analyses suggesting that different activities of the C. jejuni FlhF GTPase are required for distinct steps in flagellar gene expression and biosynthesis. Our findings are likely applicable to many polarly flagellated bacteria that utilize FlhF in flagellar biosynthesis processes.

scholarly journals Tetracycline Resistance Genes in Campylobacter jejuni and C. coli Isolated From Poultry Carcasses

2014 ◽  
Vol 7 (8) ◽  
Author(s):  
Bahman Abdi Hachesoo ◽  
Rahem Khoshbakht ◽  
Hassan Sharifi Yazdi ◽  
Mohammad Tabatabaei ◽  
Saeid Hosseinzadeh ◽  
...  
Keyword(s):  
Campylobacter Jejuni ◽  
Resistance Genes ◽  
Tetracycline Resistance ◽  
Tetracycline Resistance Genes

scholarly journals Tetracycline Resistance Gene Profiles in Red Seabream (Pagrus major) Intestine and Rearing Water After Oxytetracycline Administration

2020 ◽  
Vol 11 ◽  
Author(s):  
Yumiko Obayashi ◽  
Aya Kadoya ◽  
Naoto Kataoka ◽  
Kazuki Kanda ◽  
Su-Min Bak ◽  
...  
Keyword(s):  
Resistance Gene ◽  
Tetracycline Resistance ◽  
Pagrus Major ◽  
Tetracycline Resistance Gene ◽  
Red Seabream ◽  
Gene Profiles

scholarly journals Novel aerobic tetracycline resistance gene that chemically modifies tetracycline.

1989 ◽  
Vol 171 (1) ◽  
pp. 148-153 ◽  
Author(s):  
B S Speer ◽  
A A Salyers
Keyword(s):  
Resistance Gene ◽  
Tetracycline Resistance ◽  
Tetracycline Resistance Gene
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