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The AMPylase FIC-1 modulates TGF-β signaling in .
Front Mol Neurosci
November 2022
Neuroscience Graduate Program, University of Michigan, Ann Arbor, MI, United States.
Post-translational protein modifications are essential for the spatio-temporal regulation of protein function. In this study, we examine how the activity of the AMPylase FIC-1 modulates physiological processes . We find that over-expression (OE) of the constitutive AMPylase FIC-1(E274G) impairs development, fertility, and stress resilience.
View Article and Find Full Text PDFEvolutionary Diversification of Host-Targeted Effectors Proteins Derived from a Conserved FicTA Toxin-Antitoxin Module.
Microorganisms
July 2021
Biozentrum, University of Basel, 4056 Basel, Switzerland.
Proteins containing a FIC domain catalyze AMPylation and other post-translational modifications (PTMs). In bacteria, they are typically part of FicTA toxin-antitoxin modules that control conserved biochemical processes such as topoisomerase activity, but they have also repeatedly diversified into host-targeted virulence factors. Among these, effector proteins (Beps) comprise a particularly diverse ensemble of FIC domains that subvert various host cellular functions.
View Article and Find Full Text PDFA Bacterial Toxin Perturbs Intracellular Amino Acid Balance To Induce Persistence.
mBio
February 2021
Department of Developmental Biology, Stanford University School of Medicine, Stanford, California, USA
Bacterial cells utilize toxin-antitoxin systems to inhibit self-reproduction, while maintaining viability, when faced with environmental challenges. The activation of the toxin is often coupled to the induction of cellular response pathways, such as the stringent response, in response to multiple stress conditions. Under these conditions, the cell enters a quiescent state referred to as dormancy or persistence.
View Article and Find Full Text PDFSynthesis, antibacterial action, and ribosome inhibition of deoxyspectinomycins.
J Antibiot (Tokyo)
June 2021
Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN, USA.
Spectinomycin, an aminocyclitol antibiotic, is subject to inactivation by aminoglycoside modifying enzymes (AMEs) through adenylylation or phosphorylation of the 6-hydroxy group position. In this study, the effects of deoxygenation of the 2- and 6-hydroxy group positions on the spectinomycin actinamine ring are probed to evaluate their relationship to ribosomal binding and the antimicrobial activities of spectinomycin, semisynthetic aminomethyl spectinomycins (amSPCs), and spectinamides. To generate these analogs, an improved synthesis of 6-deoxyspectinomycin was developed using the Barton deoxygenation reaction.
View Article and Find Full Text PDFHEPN-MNT Toxin-Antitoxin System: The HEPN Ribonuclease Is Neutralized by OligoAMPylation.
Mol Cell
December 2020
Institute of Biotechnology, Life Sciences Center, Vilnius University, Sauletekio av. 7, 10257 Vilnius, Lithuania. Electronic address:
Prokaryotic toxin-antitoxin (TA) systems are composed of a toxin capable of interfering with key cellular processes and its neutralizing antidote, the antitoxin. Here, we focus on the HEPN-MNT TA system encoded in the vicinity of a subtype I-D CRISPR-Cas system in the cyanobacterium Aphanizomenon flos-aquae. We show that HEPN acts as a toxic RNase, which cleaves off 4 nt from the 3' end in a subset of tRNAs, thereby interfering with translation.
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