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Molecular interactions of the Golgi Reassembly and Stacking Protein (GRASP) from Saccharomyces cerevisiae

Grant number: 15/15410-5
Support type:Scholarships in Brazil - Master
Effective date (Start): January 01, 2016
Effective date (End): May 31, 2017
Field of knowledge:Biological Sciences - Biophysics - Molecular Biophysics
Principal researcher:Antonio José da Costa Filho
Grantee:Natália Aparecida Fontana
Home Institution: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto (FFCLRP). Universidade de São Paulo (USP). Ribeirão Preto , SP, Brazil

Abstract

Golgi Reassembly and Stacking Proteins (GRASPs) have been involved in a variety of functions including non-conventional secretion and organization of the structure of the Golgi apparatus. However, their precise role in each of those problems still deserves more detailed structural and functional studies at a molecular level. It is within this context that our project finds its main goal: the production of data that will allow understanding the structure-function correlation of the GRASP from S. cerevisiae (Grh1). The use of model organisms, such as S. cerevisiae, is strategic to obtain comprehensive information on the cell processes that GRASPs are taking part. We have the chance of generating knowledge in two biologically-relevant problems: (1) although GRASPs have been implicated in a broad set of functions, a definitive understanding of their functions in several organisms is far from complete; (2) detection and characterization of intrinsically disordered regions in proteins, which presents great potential of impact over the understanding of the role of intrinsically disordered proteins in cell processes. Thus, in the present project we aim at obtaining experimental data on the molecular interactions taking place during the Grh1 (GRASP from S. cerevisiae) functional cycle. To do so we will make use of a multidisciplinary and multitechnique approach involving methods of molecular biology and biochemistry as well as molecular biophysical tools, such as circular dichroism and electron magnetic resonance.

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