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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

The yeast GRASP Grh1 displays a high polypeptide backbone mobility along with an amyloidogenic behavior

Full text
Author(s):
Fontana, N. A. [1] ; Fonseca-Maldonado, R. [1, 2] ; Mendes, L. F. S. [1] ; Meleiro, L. P. [3] ; Costa-Filho, A. J. [1]
Total Authors: 5
Affiliation:
[1] Univ Sao Paulo, Dept Fis, Fac Filosofia Ciencias & Letras Ribeirao Preto, Ribeirao Preto, SP - Brazil
[2] Inst Fed Ciencia & Tecnol Sao Paulo, Jacarei, SP - Brazil
[3] Univ Sao Paulo, Dept Quim, Fac Filosofia Ciencias & Letras Ribeirao Preto, Ribeirao Preto, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: SCIENTIFIC REPORTS; v. 8, OCT 24 2018.
Web of Science Citations: 3
Abstract

GRASPs are proteins involved in cell processes that seem paradoxical: responsible for shaping the Golgi cisternae and involved in unconventional secretion mechanisms that bypass the Golgi. Despite its physiological relevance, there is still a considerable lack of studies on full-length GRASPs. Our group has previously reported an unexpected behavior of the full-length GRASP from the fungus C. neoformans: its intrinsically-disordered characteristic. Here, we generalize this finding by showing that it is also observed in the GRASP from S. cerevisae (Grh1), which strongly suggests it might be a general property within the GRASP family. Furthermore, Grh1 is also able to form amyloid-like fibrils either upon heating or when submitted to changes in the dielectric constant of its surroundings, a condition that is experienced by the protein when in close contact with membranes of cell compartments, such as the Golgi apparatus. Intrinsic disorder and fibril formation can thus be two structural properties exploited by GRASP during its functional cycle. (AU)

FAPESP's process: 15/18390-5 - Electron magnetic resonance in molecular biophysics: new and old looks to new and old problems
Grantee:Antonio José da Costa Filho
Support Opportunities: Regular Research Grants
FAPESP's process: 16/09676-5 - Nuclear magnetic resonance studies of the Golgi reassembly and stacking protein from Cryptococcus neoformans
Grantee:Luis Felipe Santos Mendes
Support Opportunities: Scholarships abroad - Research Internship - Doctorate (Direct)
FAPESP's process: 15/50366-7 - Resolving mechanistic details of peptide transport across membranes using crystallographic and non-crystallographic structural biology approaches
Grantee:Antonio José da Costa Filho
Support Opportunities: Regular Research Grants
FAPESP's process: 12/13309-7 - Structural and functional studies of the Golgi Re-Assembly and Stacking Protein (GRASP) from Cryptococcus neoformans
Grantee:Luis Felipe Santos Mendes
Support Opportunities: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 12/20367-3 - Structural and functional studies of the Golgi Re-Assembly and Stacking Protein (GRASP) from Cryptococcus neoformans
Grantee:Antonio José da Costa Filho
Support Opportunities: Regular Research Grants
FAPESP's process: 16/23863-2 - Molecular interactions of the Golgi Reassembly and Stacking Protein (GRASP) form Saccharomyces cerevisiae
Grantee:Natália Aparecida Fontana
Support Opportunities: Scholarships in Brazil - Doctorate (Direct)