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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.)

Disorder-to-order transitions in the molten globule-like Golgi Reassembly and Stacking Protein

Full text
Author(s):
Mendes, Luis F. S. [1] ; Basso, Luis G. M. [1] ; Kumagai, Patricia S. [2] ; Fonseca-Maldonado, Raquel [1, 3] ; Costa-Filho, Antonio J. [1]
Total Authors: 5
Affiliation:
[1] Univ Sao Paulo, Lab Biofis Mol, Dept Fis, Fac Filosofia Ciencias & Letras Ribeirao Preto, Ribeirao Preto, SP - Brazil
[2] Univ Sao Paulo, Inst Fis Sao Carlos, Grp Biofis Mol Sergio Mascarenhas, Sao Carlos, SP - Brazil
[3] Inst Fed Sao Paulo, Campus Jacarei, Jacarei, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS; v. 1862, n. 4, p. 855-865, APR 2018.
Web of Science Citations: 4
Abstract

Background: Golgi Reassembly and Stacking Proteins (GRASPs) are widely spread among eukaryotic cells (except plants) and are considered as key components in both the stacking of the Golgi cisternae and its lateral connection. Furthermore, GRASPs were also proved essential in the unconventional secretion pathway of several proteins, even though the mechanism remains obscure. It was previously observed that the GRASP homologue in Cryptococcus neoformans has a molten globule-like behavior in solution. Methods: We used circular dichroism, synchrotron radiation circular dichroism and steady-state as well as time resolved fluorescence. Results: We report the disorder-to-order transition propensities for a native molten globule-like protein in the presence of different mimetics of cell conditions. Changes in the dielectric constant (such as those experienced close to the membrane surface) seem to be the major factor in inducing multiple disorder-to-order transitions in GRASP, which shows very distinct behavior when in conditions that mimic the vicinity of the membrane surface as compared to those found when free in solution. Other folding factors such as molecular crowding, counter ions, pH and phosphorylation exhibit lower or no effect on GRASP secondary structure and/or stability. General significance: To the best of our knowledge, this is the first study focusing on understanding the disorder-to-order transitions of a molten globule structure without the need of any mild denaturing condition. A model is also introduced aiming at describing how the cell could manipulate the GRASP sensitivity to changes in the dielectric constant during different cell-cycle periods. (AU)

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 type: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 14/00206-0 - Structure and function of SARS-CoV spike glycoprotein fusion peptides
Grantee:Luís Guilherme Mansor Basso
Support type: Scholarships in Brazil - Post-Doctorate
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 type: Regular Research Grants
FAPESP's process: 11/21767-2 - Molecular interactions in the mechanism of action of human galectin-4
Grantee:Patricia Suemy Kumagai
Support type: 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 type: Regular Research Grants
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 type: Regular Research Grants