| Grant number: | 18/19992-7 |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |
| Start date: | February 01, 2019 |
| End date: | December 17, 2023 |
| Field of knowledge: | Biological Sciences - Biophysics - Molecular Biophysics |
| Principal Investigator: | Richard Charles Garratt |
| Grantee: | Italo Augusto Cavini |
| Host Institution: | Instituto de Física de São Carlos (IFSC). Universidade de São Paulo (USP). São Carlos , SP, Brazil |
| Associated research grant: | 20/02897-1 - Septin filaments: structure, polymerization and role in pathologies, AP.TEM |
| Associated research grant(s): | 24/23432-8 - Septins: Spatial Regulators of Cell Biology, AR.EXT |
| Associated scholarship(s): | 22/00262-4 - Structural studies on heteromeric septin coiled coils by high-resolution nuclear magnetic resonance spectroscopy, BE.EP.PD |
Abstract Septins constitute a conserved guanine-binding protein family which are involved in several cellular processes and are capable of self-assembling into heterofilaments and high-order complexes. The human septins are encoded by 13 different genes and are divided into four groups based on their similarity. The C-terminal domain of septins contains characteristic repeats of alpha-helix coiled-coils whose importance in the formation and/or maintenance of complexes is still not fully understood. To date, the first and only crystallographic structure of a septin heterocomplex, the heterofilament SEPT2-6-7 published in 2007, does not contain information on the C-terminal domains - because of the absence of electron density in these regions. The current project proposes to obtain structural information on the C-terminal domains of SEPT6 (and others of its group as SEPT8, 10, 11 and 14) and SEPT7 using nuclear magnetic resonance and X-ray crystallography techniques. Among our objectives, we aim to determine interaction patterns that stabilize the interface of the SEPT6C-7C coiled-coil heterodimer and give selectivity to the heterofilament assembly. With nuclear magnetic resonance spectroscopy, we expect to obtain eNOEs, interproton distances up to 5 Å, that will indicate the relative orientation of the heterodimer and allow solving its structure in solution. In parallel, crystallographic assays will be performed to obtain a three-dimensional model also by X-ray diffraction. A better structural knowledge of the C-terminal domains will certainly shed light on how septins organize and also on the reason why different isoforms exist in some organisms. | |
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