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Juxtanodin is an intrinsically disordered F-actin-binding protein
- Source :
- Scientific Reports, Scientific reports 2, 899 (2012). doi:10.1038/srep00899
- Publication Year :
- 2012
- Publisher :
- Nature Publishing Group, 2012.
-
Abstract
- Juxtanodin, also called ermin, is an F-actin-binding protein expressed by oligodendrocytes, the myelin-forming cells of the central nervous system. While juxtanodin carries a short conserved F-actin-binding segment at its C terminus, it otherwise shares no similarity with known protein sequences. We carried out a structural characterization of recombinant juxtanodin in solution. Juxtanodin turned out to be intrinsically disordered, as evidenced by conventional and synchrotron radiation CD spectroscopy. Small-angle X-ray scattering indicated that juxtanodin is a monomeric, highly elongated, unfolded molecule. Ensemble optimization analysis of the data suggested also the presence of more compact forms of juxtanodin. The C terminus was a strict requirement for co-sedimentation of juxtanodin with microfilaments, but juxtanodin had only mild effects on actin polymerization. The disordered nature of juxtanodin may predict functions as a protein interaction hub, although F-actin is its only currently known binding partner.
- Subjects :
- Circular dichroism
metabolism [Muscle, Skeletal]
metabolism [Recombinant Proteins]
Swine
chemistry [Recombinant Proteins]
Plasma protein binding
Microfilament
Protein Structure, Secondary
X-Ray Diffraction
juxtanodin protein, rat
Peptide sequence
Multidisciplinary
biology
Circular Dichroism
Microfilament Proteins
chemistry [Carrier Proteins]
Microfilament Protein
Recombinant Proteins
Solutions
Biochemistry
chemistry [Actins]
Algorithms
Protein Binding
F-actin-binding proteins
metabolism [Actins]
Molecular Sequence Data
macromolecular substances
chemistry [Solutions]
Article
Scattering, Small Angle
Animals
chemistry [Microfilament Proteins]
Amino Acid Sequence
Muscle, Skeletal
Actin
Sequence Homology, Amino Acid
C-terminus
ultrastructure [Actins]
metabolism [Microfilament Proteins]
Actins
Myelin basic protein
Rats
Microscopy, Electron
ddc:000
biology.protein
Biophysics
genetics [Microfilament Proteins]
Carrier Proteins
Software
metabolism [Carrier Proteins]
Subjects
Details
- Language :
- English
- ISSN :
- 20452322
- Database :
- OpenAIRE
- Journal :
- Scientific Reports
- Accession number :
- edsair.doi.dedup.....af9a71d22f505cdb1bbfa1ce42a27cfa
- Full Text :
- https://doi.org/10.1038/srep00899