Rashmi Panigrahi

University of Alberta

ABSTRACT

Functional  proteins  were  often  thought  of  as  well-­‐folded  molecules  with  unique  three-dimensional structures. However, in the last few decades, disordered domains have increasingly intrigued biologists. These so-­‐called “intrinsically disordered regions (IDRs)” do not fit to the “lock and key"  hypothesis proposed by Emil Fischer, highlighting that  stable  three-dimensional structure is not prerequisite for functionality. In transmembrane proteins, IDRs are involved in regulating protein activity. Further, they are known to have a number of phosphorylated residues and interact with more partners compared to their folded counterparts. In this study, we discuss the regulatory role of such intrinsically disordered cytosolic domain of intramembrane enzyme Diacyglycerol acyltransferase1.  combinatorial approach using biophysical and biochemical tools has been undertaken to gain the structure-function insight of this disorder. We have used SSRL BioSAXS beamline for this study, alongside NMR and enzyme activity analysis.
References

1. Rashmi Panigrahi, Tsutomu Matsui, Andrew H. Song, Kristian Mark P. Caldo, Howard S. Young, Randall J. Weselake, M. Joanne Lemieux (2018)   Intrinsic disorder in the regulatory N-terminal domain of Diacylglycerol acyltransferase 1 from Brassica napus. Scientific Reports 8:16665

 2. Kristian  Mark P. Caldo, Jeella Z. Acedo, Rashmi Panigrahi, John C. Vederas, Randall J. Weselake and M. Joanne Lemieux (2017) Diacylglycerol Acyl transferase 1 is regulated by its N-‐terminal domain in response to allosteric effectors. Plant Physiology, 175(2): 667-­‐680

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Email: panigrah@ualberta.ca