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Accepted (AM)Open Access (License Unspecified), Open
Journal article
Versatility of Acyl-Acyl Carrier Protein Synthetases
Chemistry & biology, v 21(10), pp 1293-1299
23 Oct 2014
PMID: 25308274
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The acyl carrier protein (ACP) requires posttranslational modification with a 4′-phosphopantetheine arm for activity, and this thiol-terminated modification carries cargo between enzymes in ACP-dependent metabolic pathways. We show that acyl-ACP synthetases (AasSs) from different organisms are able to load even, odd, and unnatural fatty acids onto E. coli ACP in vitro. Vibrio harveyi AasS not only shows promiscuity for the acid substrate, but also is active upon various alternate carrier proteins. AasS activity also extends to functional activation in living organisms. We show that exogenously supplied carboxylic acids are loaded onto ACP and extended by the E. coli fatty acid synthase, including unnatural fatty acid analogs. These analogs are further integrated into cellular lipids. In vitro characterization of four different adenylate-forming enzymes allowed us to disambiguate CoA-ligases and AasSs, and further in vivo studies show the potential for functional application in other organisms.
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•Efficient loading of various acids on acyl carrier protein (ACP) using AasS•Acylation of ACPs with AasS from different pathways and organisms•Uptake, acylation, and extension of unnatural acids in vivo, catalyzed by AasS
A novel small-molecule inhibitor of myogenic miRNAs (myomiRs) was identified, which was further applied as a small-molecular probe that revealed a novel miR-221/222-myoD-myomiRs regulatory pathway.
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Details
- Title
- Versatility of Acyl-Acyl Carrier Protein Synthetases
- Creators
- Joris Beld - University of California San DiegoKara Finzel - University of California San DiegoMichael D. Burkart - University of California San DiegoUniv. of California, San Diego, CA (United States)
- Publication Details
- Chemistry & biology, v 21(10), pp 1293-1299
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Microbiology and Immunology
- Web of Science ID
- WOS:000344521300008
- Scopus ID
- 2-s2.0-84908317493
- Other Identifier
- 991020535055104721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology