ArticleScientific reports2018
Intrinsic disorder in the regulatory N-terminal domain of diacylglycerol acyltransferase 1 from Brassica napus.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Adaptable SEC-SAXS data collection for higher quality structure analysis in solution.Protein science : a publication of the Protein Society · 2024Article
- Mapping allosteric pathway in NIa-Pro using computational approach.Quantitative biology (Beijing, China) · 2023Article
- Acyl-CoA-dependent and acyl-CoA-independent avocado acyltransferases positively influence oleic acid content in nonseed triacylglycerols.Frontiers in plant science · 2022Article
- Functional characterization of two type-1 diacylglycerol acyltransferase (DGAT1) genes from rice (Oryza sativa) embryo restoring the triacylglycerol accumulation in yeast.Plant molecular biology · 2021Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
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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