Structural disorder and local order of hNopp140

Tantos, Ágnes and Szrnka, Krisztina and Szabó, Beáta and Bokor, Mónika Zsuzsanna and Kamasa, Pawel and Matus, Péter and Békési, Angéla and Tompa, Kálmán and Han, Kyou-Hoon and Tompa, Péter (2013) Structural disorder and local order of hNopp140. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1834 (1). pp. 342-350. ISSN 1570-9639

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Human nucleolar phosphoprotein p140 (hNopp 140) is a highly phosphorylated protein inhibitor of casein kinase 2 (CK2). As in the case of many kinase-inhibitor systems, the inhibitor has been described to belong to the family of intrinsically disordered proteins (IDPs), which often utilize transient structural elements to bind their cognate enzyme. Here we investigated the structural status of this protein both to provide distinct lines of evidence for its disorder and to point out its transient structure potentially involved in interactions and also its tendency to aggregate. Structural disorder of hNopp140 is apparent by its anomalous electrophoretic mobility, protease sensitivity, heat stability, hydrodynamic behavior on size-exclusion chromatography, 1HNMR spectrum and differential scanning calorimetry scan. hNopp140 has a significant tendency to aggregate and the change of its circular dichroism spectrum in the presence of 0–80% TFE suggests a tendency to formlocal helical structures.Wide-line NMRmeasurements suggest the overall disordered character of the protein. In all, our data suggest that this protein falls into the pre-molten globule state of IDPs, with a significant tendency to become ordered in the presence of its partner as demonstrated in the presence of transcription factor IIB (TFIIB).

Item Type: Article
Uncontrolled Keywords: Intrinsically disordered protein, Human nucleolar phosphoprotein p140, Pre-structured motif, Local structure
Subjects: Q Science / természettudomány > QH Natural history / természetrajz > QH301 Biology / biológia
Depositing User: MTMT SWORD
Date Deposited: 13 Nov 2013 13:39
Last Modified: 06 Oct 2015 19:26

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