Journal
SCIENTIFIC REPORTS
Volume 8, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41598-018-34339-1
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Funding
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- DOE Office of Biological and Environmental Research
- National Institutes of Health, National Institute of General Medical Sciences [P41GM103393]
- Canadian Institute for Health Research (CIHR)
- Alberta Innovates Health Solutions (AIHS)
- Heart and Stroke Foundation of Canada
- Deutsche Forschungsgemeinschaft (DFG) [1830]
- Natural Sciences and Engineering Research Council's International Research Training Group in Membrane Biology
- Alberta Innovates Technology Futures Graduate Scholarship
- Alberta Canola Producers Commission Graduate Award (KMPC)
- Canada Research Chairs Program
- Alberta Innovates Health Solutions Scholars program
- Natural Sciences and Engineering Research Council of Canada (NSERC) [RGPIN-2016-06478, RGPIN-2014-04585]
- Canadian Foundation for Innovation
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P41GM103393] Funding Source: NIH RePORTER
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Proteins with multifunctional regulatory domains often demonstrate structural plasticity or protein disorder, allowing the binding of multiple regulatory factors and post-translational modifications. While the importance of protein disorder is clear, it also poses a challenge for in vitro characterization. Here, we report protein intrinsic disorder in a plant molecular system, which despite its prevalence is less studied. We present a detailed biophysical characterization of the entire cytoplasmic N-terminal domain of Brassica napus diacylglycerol acyltransferase, (DGAT1), which includes an inhibitory module and allosteric binding sites. Our results demonstrate that the monomeric N-terminal domain can be stabilized for biophysical characterization and is largely intrinsically disordered in solution. This domain interacts with allosteric modulators of DGAT1, CoA and oleoyl-CoA, at micromolar concentrations. While solution scattering studies indicate conformational heterogeneity in the N-terminal domain of DGAT1, there is a small gain of secondary structure induced by ligand binding.
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