Kamal K. Joshi/sandbox 1
From Proteopedia
Introduction
RcdA was first identified as a regulator for CtrA degradation, a master regulator in Caulobacter crescentus (McGrath et al., 2006). It was shown to be important for the regulated degradation of CtrA, a replication inhibitor and transcriptional activator, during swarmer to stalked transition of Caulobacter life cycle. Later in 2009, its crystal structure was solved at 2.9 A resolution(Taylor et al., 2009) yet the true function of RcdA has not been assigned. We are working towards understanding the role of RcdA during regulated proteolysis of substrate proteins in the model organism Caulobacter [[1]]
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Biological state of RcdA
RcdA exist as a homodimer in solution shown by size exclusion chromatography as well as by crystal structure (Taylor et al., 2009). The monomeric unit consists of a three-helix bundle with three disordered regions. Both monomeric units pack each other in a 2-fold symmetric orientation.
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Conservation of RcdA
RcdA is conserved across gram-negative alpha-proteobacteria. This further lead us to hypothesize that RcdA is playing an important role in the regulatory processes in Caulobacter. The conservation of different residues as predicted by Consurf software are shown in the diagram. The color scheme representing the degree of conservation is shown below.
References: 1. Patrick T. McGrath, Antonio A. Iniesta, Kathleen R. Ryan, Lucy Shapiro and Harley H. McAdams. " A Dynamically Localized Protease Complex and a Polar Specificity Factor Control a Cell Cycle Master Regulator". Cell, (2006) 124, 535–547. 2. James A. Taylor, Jeremy D. Wilbur, Stephen C. Smith and Kathleen R. Ryan. "Mutations that Alter RcdA Surface Residues Decouple Protein Localization and CtrA Proteolysis in Caulobacter crescentus". J. Mol. Biol. (2009) 394,46–60.
