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Association between the intrinsically disordered protein PEX19 and PEX3
Katarina Hattula1, Daniel Hirschberg1, Nisse Kalkkinen1
1Institute of Biotechnology, University of Helsinki, Helsinki, Finland.
Plos One
|July 26, 2014
Summary
Peroxins 3 and 19 (PEX3 and PEX19) are crucial for peroxisome formation. Hydrogen exchange mass spectrometry revealed PEX19 stabilizes PEX3, preventing its aggregation through specific binding interactions.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Peroxins (PEXs) 3 and 19 are essential for early peroxisomal biogenesis.
- Understanding the interaction between PEX3 and PEX19 is key to elucidating peroxisome assembly.
Purpose of the Study:
- To investigate the conformational changes during the in vitro interaction of PEX3 and PEX19.
- To characterize the binding interface and stabilization mechanisms between PEX3 and PEX19.
Main Methods:
- Hydrogen exchange mass spectrometry (HX-MS) was employed to monitor protein dynamics.
- In vitro complex formation between purified PEX3 and PEX19 was analyzed.
Main Results:
- PEX19 exhibited flexibility upon binding to PEX3, with specific regions (N-terminus, C-terminus, F64-L74) becoming shielded from hydrogen exchange.
- PEX3 showed increased protection from hydrogen exchange within the PEX19 binding groove.
- The N-terminus of PEX19 likely initiates binding, followed by stabilization through helix and core folding, enhancing affinity.
Conclusions:
- PEX19 binding stabilizes PEX3, preventing its aggregation within the cell.
- The interaction involves sequential conformational changes in both PEX3 and PEX19, leading to high-affinity complex formation.
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