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Structural determination of the C-terminal domains of septins SEPT2 and SEPT4 and protein interaction with alpha-synuclein by NMR

Grant number: 10/12953-4
Support type:Scholarships in Brazil - Post-Doctorate
Effective date (Start): December 01, 2010
Effective date (End): November 30, 2013
Field of knowledge:Biological Sciences - Biophysics - Molecular Biophysics
Principal Investigator:Richard Charles Garratt
Grantee:Edson Crusca Junior
Home Institution: Instituto de Física de São Carlos (IFSC). Universidade de São Paulo (USP). São Carlos , SP, Brazil
Associated research grant:08/57910-0 - National Institute of Structural Biotechnology and Medicinal Chemistry in Infectious Diseases, AP.TEM

Abstract

Septins are a conserved family of binding proteins to guanine nucleotide which are involved in many cellular processes. The functions of these proteins are probably a result from their inherent ability to assemble into complexes and form highly ordered polymers. These complexes can act as diffusion barriers for the compartmentalization of the cell membrane, vesicle trafficking and ways of protein interaction to specific intracelular locations. The sequences of all members of this family can be divided into three distinct domains: a N-terminal variable domain, a central GTPase domain and a C-terminal domain that typically includes sequences characteristic of coiled-coils.Some septins are related to pathological states, for example, septins SEPT1, SEPT2 and SEPT4 appear to accumulate in filamentous deposits (Lewy bodies) in Alzheimer's disease; SEPT4 was also co-located with the protein alpha-synuclein in Parkinson disease. Specific combinations of septins form hetero-oligomeric complexes that polymerize into non-polar filaments in vivo and in vitro. The complex formed by the human septins SEPT2, SEPT6 and SEPT7 was solved by Sirajuddin et al. (2007) by X-ray crystallography. However, the C-terminal domains do not presented electron density in the crystal structure, providing no information about these parts of the complex which may be critical for determining the way that different septins interact in the assembly of hetero-oligomeric complexes. As the main purpose of this project is intended to characterize, by means of nuclear magnetic resonance, the structure and dynamics of the C-terminal domains of human septins SEpt4 SEPT2 and in the process of formation of homo-and hetero-dimers. (AU)

Scientific publications (5)
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
ERLACH, MARKUS BECK; KOEHLER, JOERG; MUNTE, CLAUDIA E.; KREMER, WERNER; CRUSCA, JR., EDSON; KAINOSHO, MASATSUNE; KALBITZER, HANS ROBERT. Pressure dependence of side chain(1)H and(15)N-chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH2. Journal of Biomolecular NMR, JUN 2020. Web of Science Citations: 0.
VICENTE, EDUARDO F.; SAHU, INDRA D.; CRUSCA, JR., EDSON; BASSO, LUIS G. M.; MUNTE, CLAUDIA E.; COSTA-FILHO, ANTONIO J.; LORIGAN, GARY A.; CILLI, EDUARDO M. HsDHODH Microdomain-Membrane Interactions Influenced by the Lipid Composition. Journal of Physical Chemistry B, v. 121, n. 49, p. 11085-11095, DEC 14 2017. Web of Science Citations: 1.
ERLACH, MARKUS BECK; KOEHLER, JOERG; CRUSCA, JR., EDSON; MUNTE, CLAUDIA E.; KAINOSHO, MASATSUNE; KREMER, WERNER; KALBITZER, HANS ROBERT. Pressure dependence of side chain C-13 chemical shifts in model peptides Ac-Gly-Gly-Xxx-Ala-NH2. Journal of Biomolecular NMR, v. 69, n. 2, p. 53-67, OCT 2017. Web of Science Citations: 3.
BASSO, LUIS G. M.; VICENTE, EDUARDO F.; CRUSCA, JR., EDSON; CILLI, EDUARDO M.; COSTA-FILHO, ANTONIO J. SARS-CoV fusion peptides induce membrane surface ordering and curvature. SCIENTIFIC REPORTS, v. 6, NOV 28 2016. Web of Science Citations: 9.
ERLACH, MARKUS BECK; KOEHLER, JOERG; CRUSCA, JR., EDSON; KREMER, WERNER; MUNTE, CLAUDIA E.; KALBITZER, HANS ROBERT. Pressure dependence of backbone chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH2. Journal of Biomolecular NMR, v. 65, n. 2, p. 65-77, JUN 2016. Web of Science Citations: 7.

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