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Solution structure and flexibility of the condensin HEAT-repeat subunit Ycg1
Karen Manalastas-Cantos1, Marc Kschonsak2, Christian H Haering2
1European Molecular Biology Laboratory, Hamburg Unit, Hamburg 22607, Germany.
The Journal of Biological Chemistry
|July 28, 2019
Summary
The condensin subunit Ycg1 is flexible alone but rigidifies upon binding Brn1. SAXS analysis reveals Ycg1 oligomerization and models its conformational changes for DNA binding.
Area of Science:
- Structural biology
- Biochemistry
- Molecular dynamics
Background:
- High-resolution structural analysis of flexible proteins is challenging.
- Small-angle X-ray scattering (SAXS) aids in modeling flexible protein states.
Purpose of the Study:
- To characterize the solution structure of the condensin HEAT-repeat subunit Ycg1.
- To investigate the effect of its partner protein Brn1 on Ycg1 structure and dynamics.
Main Methods:
- Small-angle X-ray scattering (SAXS).
- Dynamic and static multiangle light scattering.
- Normal mode analysis for structural modeling.
Main Results:
- Free Ycg1 is flexible in solution and tends to oligomerize.
- Ycg1 becomes more rigid when bound to Brn1.
- Models of Ycg1 monomers, dimers, and tetramers were generated.
Conclusions:
- Ycg1 undergoes conformational transitions upon Brn1 binding.
- These transitions are crucial for forming the DNA-binding surface in condensin.
Keywords:
DNA binding proteinHEAT-repeatcondensinconformational changedynamic light scattering (DLS)oligomerprotein flexibilitysize exclusion chromatography with multiangle static light scattering (SEC–MALS)small-angle X-ray scattering (SAXS)structural modelMore Related Videos
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