Structural and Thermodynamic Properties of Septin 3 Investigated by Small-Angle X-Ray Scattering
Biophysical Journal, ISSN: 0006-3495, Vol: 108, Issue: 12, Page: 2896-2902
2015
- 3Citations
- 25Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations3
- Citation Indexes3
- CrossRef2
- Captures25
- Readers25
- 25
Article Description
Septins comprise a family of proteins involved in a variety of cellular processes and related to several human pathologies. They are constituted by three structural domains: the N- and C-terminal domains, highly variable in length and composition, and the central domain, involved in the guanine nucleotide (GTP) binding. Thirteen different human septins are known to form heterogeneous complexes or homofilaments, which are stabilized by specific interactions between the different interfaces present in the domains. In this work, we have investigated by in-solution small-angle x-ray scattering the structural and thermodynamic properties of a human septin 3 construct, SEPT3-GC, which contains both of both interfaces (G and NC) responsible for septin-septin interactions. In order to shed light on the role of these interactions, small-angle x-ray scattering measurements were performed in a wide range of temperatures, from 2 up to 56°C, both with and without a nonhydrolysable form of GTP (GTP γ S). The acquired data show a temperature-dependent coexistence of monomers, dimers, and higher-order aggregates that were analyzed using a global fitting approach, taking into account the crystallographic structure of the recently reported SEPT3 dimer, PDB: 3SOP. As a result, the enthalpy, entropy, and heat capacity variations that control the dimer-monomer dissociation equilibrium in solution were derived and GTP γ S was detected to increase the enthalpic stability of the dimeric species. Moreover, a temperature increase was observed to induce dissociation of SEPT3-GC dimers into monomers just preceding their reassembling into amyloid aggregates, as revealed by the Thioflavin-T fluorescence assays.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0006349515005007; http://dx.doi.org/10.1016/j.bpj.2015.05.015; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84931275606&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/26083929; https://linkinghub.elsevier.com/retrieve/pii/S0006349515005007; http://www.cell.com/biophysj/abstract/S0006-3495(15)00500-7
Elsevier BV
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