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The irreversible dodecamerization of native Dps trimers from Mycobacterium smegmatis, in vitro, is known to be directly associated with the bimodal function of this protein. Hence it is important to explore this pathway at the molecular level. Two types of trimers, Trimer A (tA) and Trimer B (tB), can be derived from the dodecamer due to the inherent 3-fold symmetry of the spherical crystal structure. These derived trimers were expressed as protein structure graphs (PSGs) using the computed interaction strength among the residues. Interface clusters which were identified from PSGs allowed us to convincingly predict E146 and F47 for further mutation studies. Various single and double mutants were constructed and characterized. We were finally able to generate a single mutant F47E impaired in dodecamerization and a double mutant E146AF47E as native monomer in solution. These two observed results suggest that the two trimers are important for dodecamerization and that the residues selected are important for the structural stability of the protein in vitro.

biochemistry

Molecular Mechanism of <i>in Vitro</i> Oligomerization of Dps from <i>Mycobacterium smegmatis:</i> Mutations of the Residues Identified by “Interface Cluster” Analysis

Molecular Mechanism of in Vitro Oligomerization of Dps from Mycobacterium smegmatis: Mutations of the Residues Identified by “Interface Cluster” Analysis