Solution structure and flexibility of the condensin HEAT-repeat subunit Ycg1.

ABSTRACT: High-resolution structural analysis of flexible proteins is frequently challenging and requires the synergistic application of different experimental techniques. For these proteins, small-angle X-ray scattering (SAXS) allows for a quantitative assessment and modeling of potentially flexible and heterogeneous structural states. Here, we report SAXS characterization of the condensin HEAT-repeat subunit Ycg1^Cnd3 in solution, complementing currently available high-resolution crystallographic models. We show that the free Ycg1 subunit is flexible in solution but becomes considerably more rigid when bound to its kleisin-binding partner protein Brn1^Cnd2 The analysis of SAXS and dynamic and static multiangle light scattering data furthermore reveals that Ycg1 tends to oligome

SUBMITTER: Manalastas-Cantos K 

PROVIDER: S-EPMC6746440 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature