ArticleThe Journal of biological chemistry2012
Cyclic AMP-induced conformational changes in mycobacterial protein acetyltransferases.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 25 citations in OpenAlex.
- Review
- Negative regulation of the acsA1 gene encoding the major acetyl-CoA synthetase by cAMP receptor protein in Mycobacterium smegmatis.Journal of microbiology (Seoul, Korea) · 2022Article
- Expression of a novel mycobacterial phosphodiesterase successfully lowers cAMP levels resulting in reduced tolerance to cell wall-targeting antimicrobials.The Journal of biological chemistry · 2022Article
- Post-translational Succinylation ofACS infectious diseases · 2020Article
- A universal stress protein inThe Journal of biological chemistry · 2020Article
- More than cholesterol catabolism: regulatory vulnerabilities in Mycobacterium tuberculosis.Current opinion in chemical biology · 2018Review
- Hybrid Mass Spectrometry Approaches to Determine How L-Histidine Feedback Regulates the Enzyzme MtATP-Phosphoribosyltransferase.Structure (London, England : 1993) · 2017Article
- Regulation of a Protein Acetyltransferase in Myxococcus xanthus by the Coenzyme NADP.Journal of bacteriology · 2015Article
- Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress.Microbiology and molecular biology reviews : MMBR · 2015Review
- Novel inhibitors of cholesterol degradation in Mycobacterium tuberculosis reveal how the bacterium's metabolism is constrained by the intracellular environment.PLoS pathogens · 2015Article
- Applications of hydrogen/deuterium exchange MS from 2012 to 2014.Analytical chemistry · 2015Review
- Acetylome analysis reveals diverse functions of lysine acetylation in Mycobacterium tuberculosis.Molecular & cellular proteomics : MCP · 2014Article
- Novel binding motif and new flexibility revealed by structural analyses of a pyruvate dehydrogenase-dihydrolipoyl acetyltransferase subcomplex from the Escherichia coli pyruvate dehydrogenase multienzyme complex.The Journal of biological chemistry · 2014Article
- Allostery and conformational dynamics in cAMP-binding acyltransferases.The Journal of biological chemistry · 2014Article
- Structure and function of the catalytic domain of the dihydrolipoyl acetyltransferase component in Escherichia coli pyruvate dehydrogenase complex.The Journal of biological chemistry · 2014Article
- Insight to the interaction of the dihydrolipoamide acetyltransferase (E2) core with the peripheral components in the Escherichia coli pyruvate dehydrogenase complex via multifaceted structural approaches.The Journal of biological chemistry · 2013Article
- Cyclic AMP-dependent protein lysine acylation in mycobacteria regulates fatty acid and propionate metabolism.The Journal of biological chemistry · 2013Article
- Cyclic AMP regulation of protein lysine acetylation in Mycobacterium tuberculosis.Nature structural & molecular biology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The activities of a number of proteins are regulated by the binding of cAMP and cGMP to cyclic nucleotide binding (CNB) domains that are found associated with one or more effector domains with diverse functions. Although the conserved architecture of CNB domains has been extensively studied by x-ray crystallography, the key to unraveling the mechanisms of cAMP action has been protein dynamics analyses. Recently, we have identified a novel cAMP-binding protein from mycobacteria, where cAMP regulates the activity of an associated protein acetyltransferase domain. In the current study, we have monitored the conformational changes that occur upon cAMP binding to the CNB domain in these proteins, using a combination of bioluminescence resonance energy transfer and amide hydrogen/deuterium exchange mass spectrometry. Coupled with mutational analyses, our studies reveal the critical role of the linker region (positioned between the CNB domain and the acetyltransferase domain) in allosteric coupling of cAMP binding to activation of acetyltransferase catalysis. Importantly, major differences in conformational change upon cAMP binding were accompanied by stabilization of the CNB and linker domain alone. This is in contrast to other cAMP-binding proteins, where cyclic nucleotide binding has been shown to involve intricate and parallel allosteric relays. Finally, this powerful convergence of results from bioluminescence resonance energy transfer and hydrogen/deuterium exchange mass spectrometry reaffirms the power of solution biophysical tools in unraveling mechanistic bases of regulation of proteins in the absence of high resolution structural information.
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