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Published on: September 26, 2014
Structural disorder and local order of hNopp140
Agnes Tantos1, Kriszta Szrnka, Beata Szabo
1Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary.
Biochimica Et Biophysica Acta
|August 22, 2012
Summary
Human nucleolar phosphoprotein p140 (hNopp140), an intrinsically disordered protein (IDP), inhibits casein kinase 2 (CK2). This study confirms hNopp140
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Human nucleolar phosphoprotein p140 (hNopp140) is a key inhibitor of casein kinase 2 (CK2).
- Intrinsically disordered proteins (IDPs) often exhibit transient structures crucial for enzyme interactions.
- Understanding hNopp140's structure is vital for elucidating its regulatory role.
Purpose of the Study:
- To provide evidence for the intrinsically disordered nature of hNopp140.
- To identify transient structural elements involved in protein interactions.
- To investigate the aggregation propensity of hNopp140.
Main Methods:
- Electrophoresis
- Protease sensitivity assays
- Size-exclusion chromatography
- Nuclear Magnetic Resonance (NMR) spectroscopy (1H and wide-line)
- Differential Scanning Calorimetry (DSC)
- Circular Dichroism (CD) spectroscopy with TFE titration
Main Results:
- Multiple biophysical techniques confirmed the disordered state of hNopp140.
- hNopp140 exhibits a propensity to aggregate.
- Evidence suggests local helical structure formation in the presence of TFE.
- NMR data indicate an overall disordered character, consistent with a pre-molten globule state.
- Binding with transcription factor IIB (TFIIB) induced ordered structural changes.
Conclusions:
- hNopp140 is an intrinsically disordered protein in a pre-molten globule state.
- The protein possesses a tendency for aggregation and can form transient helical structures.
- Interactions with partners like TFIIB can induce order in hNopp140 structure.
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