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Effect of Phosphory...
Effect of Phosphorylation on a Human-like Osteopontin Peptide
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- Lenton, Samuel (author)
- Keele University,University of Leeds,Institut Laue Langevin
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- Grimaldo, Marco (author)
- University of Tübingen,Institut Laue Langevin
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- Roosen-Runge, Felix (author)
- Lund University,Lunds universitet,Fysikalisk kemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Physical Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,Institut Laue Langevin
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- Schreiber, Frank (author)
- University of Tübingen
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- Nylander, Tommy (author)
- Lund University,Lunds universitet,Fysikalisk kemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Physical Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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- Clegg, Roger (author)
- Hannah Research Institute
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- Holt, Carl (author)
- University of Glasgow
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- Härtlein, Michael (author)
- Institut Laue Langevin
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- García Sakai, Victoria (author)
- Rutherford Appleton Laboratory
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- Seydel, Tilo (author)
- Institut Laue Langevin
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- Marujo Teixeira, Susana C. (author)
- National Institute of Standards and Technology (NIST),University of Delaware
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(creator_code:org_t)
- Elsevier BV, 2017
- 2017
- English 11 s.
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In: Biophysical Journal. - : Elsevier BV. - 0006-3495. ; 112:8, s. 1586-1596
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Abstract
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- The last decade established that the dynamic properties of the phosphoproteome are central to function and its modulation. The temporal dimension of phosphorylation effects remains nonetheless poorly understood, particularly for intrinsically disordered proteins. Osteopontin, selected for this study due to its key role in biomineralization, is expressed in many species and tissues to play a range of distinct roles. A notable property of highly phosphorylated isoforms of osteopontin is their ability to sequester nanoclusters of calcium phosphate to form a core-shell structure, in a fluid that is supersaturated but stable. In Biology, this process enables soft and hard tissues to coexist in the same organism with relative ease. Here, we extend our understanding of the effect of phosphorylation on a disordered protein, the recombinant human-like osteopontin rOPN. The solution structures of the phosphorylated and unphosphorylated rOPN were investigated by small-angle x-ray scattering and no significant changes were detected on the radius of gyration or maximum interatomic distance. The picosecond-to-nanosecond dynamics of the hydrated powders of the two rOPN forms were further compared by elastic and quasi-elastic incoherent neutron scattering. Phosphorylation was found to block some nanosecond side-chain motions while increasing the flexibility of other side chains on the faster timescale. Phosphorylation can thus selectively change the dynamic behavior of even a highly disordered protein such as osteopontin. Through such an effect on rOPN, phosphorylation can direct allosteric mechanisms, interactions with substrates, cofactors and, in this case, amorphous or crystalline biominerals.
Subject headings
- NATURVETENSKAP -- Biologi -- Biofysik (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biophysics (hsv//eng)
Publication and Content Type
- art (subject category)
- ref (subject category)
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- By the author/editor
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Lenton, Samuel
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Grimaldo, Marco
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Roosen-Runge, Fe ...
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Schreiber, Frank
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Nylander, Tommy
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Clegg, Roger
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show more...
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Holt, Carl
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Härtlein, Michae ...
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García Sakai, Vi ...
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Seydel, Tilo
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Marujo Teixeira, ...
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- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biophysics
- Articles in the publication
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Biophysical Jour ...
- By the university
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Lund University