Structural disorder and local order of hNopp140

Agnes Tantos, Kriszta Szrnka, Beata Szabo, M. Bokor, Pawel Kamasa, Peter Matus, Angela Bekesi, K. Tompa, Kyou Hoon Han, Peter Tompa

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

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, 1H NMR 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 form local helical structures. Wide-line NMR measurements 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).

Original languageEnglish
Pages (from-to)342-350
Number of pages9
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1834
Issue number1
DOIs
Publication statusPublished - Jan 2013

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Intrinsically Disordered Proteins
Proteins
Transcription Factor TFIIB
Nuclear magnetic resonance
Casein Kinase II
Electrophoretic mobility
Size exclusion chromatography
Phosphoproteins
Differential Scanning Calorimetry
Polytetrafluoroethylene
Hydrodynamics
Circular Dichroism
Gel Chromatography
Molten materials
Differential scanning calorimetry
Peptide Hydrolases
Phosphotransferases
Hot Temperature
Enzymes
Proton Magnetic Resonance Spectroscopy

Keywords

  • Human nucleolar phosphoprotein p140
  • Intrinsically disordered protein
  • Local structure
  • Pre-structured motif

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Analytical Chemistry
  • Molecular Biology

Cite this

Structural disorder and local order of hNopp140. / Tantos, Agnes; Szrnka, Kriszta; Szabo, Beata; Bokor, M.; Kamasa, Pawel; Matus, Peter; Bekesi, Angela; Tompa, K.; Han, Kyou Hoon; Tompa, Peter.

In: Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1834, No. 1, 01.2013, p. 342-350.

Research output: Contribution to journalArticle

Tantos, A, Szrnka, K, Szabo, B, Bokor, M, Kamasa, P, Matus, P, Bekesi, A, Tompa, K, Han, KH & Tompa, P 2013, 'Structural disorder and local order of hNopp140', Biochimica et Biophysica Acta - Proteins and Proteomics, vol. 1834, no. 1, pp. 342-350. https://doi.org/10.1016/j.bbapap.2012.08.005
Tantos, Agnes ; Szrnka, Kriszta ; Szabo, Beata ; Bokor, M. ; Kamasa, Pawel ; Matus, Peter ; Bekesi, Angela ; Tompa, K. ; Han, Kyou Hoon ; Tompa, Peter. / Structural disorder and local order of hNopp140. In: Biochimica et Biophysica Acta - Proteins and Proteomics. 2013 ; Vol. 1834, No. 1. pp. 342-350.
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