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The chaperome: study of the relationship of the structure of its components and the maintenance of proteostasis

Grant number: 17/26131-5
Support type:Research Projects - Thematic Grants
Duration: March 01, 2019 - February 28, 2025
Field of knowledge:Biological Sciences - Biochemistry - Chemistry of Macromolecules
Principal researcher:Carlos Henrique Inacio Ramos
Grantee:Carlos Henrique Inacio Ramos
Home Institution: Instituto de Química (IQ). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil
Pesquisadores principais:
Julio Cesar Borges ; Leandro Ramos Souza Barbosa
Assoc. researchers:Denize Cristina Favaro ; Leandro Ramos Souza Barbosa ; Lisandra Marques Gava Borges
Associated scholarship(s):22/09729-2 - Technical assistance in the development of research linked to a thematic project., BP.TT
22/08855-4 - Study of interactions between chaperome components, BP.PD
22/08968-3 - Technical assitance in Thematic Project., BP.TT
+ associated scholarships 22/07497-7 - Technical assistance: Chaperome., BP.TT
22/02672-5 - THE CHAPEROME: STUDY OF THE RELATIONSHIP OF THE STRUCTURE OF ITS COMPONENTS AND THE MAINTENANCE OF PROTEOSTASIS, BP.TT
21/02289-4 - Structural studies of the Activator of HSP90 ATPase (Aha) co-chaperone isoforms in Plasmodium falciparum in complex with the HSP90 chaperone and characterization of their cellular roles, BP.PD
20/15947-7 - Mapping and mechanistic characterization of the interaction of the human HspA5 (BiP/Grp78/erHsp70) protein with the human Hep1 co-chaperone and with the Spike protein of the SARS-CoV-2 Coronavirus, BP.PD
21/04799-0 - Functional and structural characterization of truncated mutants of human Hsp70-escort protein 1, BP.IC
21/02629-0 - The chaperome: study of the relationship of the structure of its components and the maintenance of proteostasis, BP.TT
20/11645-6 - Conformational and functional characterization of Aedes aegypti Hsp70 chaperone, BP.IC
19/22422-0 - Cellular functional study of high molecular weight oligomers of mortaline and the effects of mitochondrial co-chaperones on their structure, BP.PD
19/16114-1 - Structure / function relationship of the Hsp40s., BP.PD
19/14209-5 - Analysis and characterization of the n- and C- terminal domains of human BiP protein (HspA5), BP.IC
19/09370-1 - THE CHAPEROME: STUDY OF THE RELATIONSHIP OF THE STRUCTURE OF ITS COMPONENTS AND THE MAINTENANCE OF PROTEOSTASIS, BP.TT
19/09371-8 - The chaperome: study of the relationship of the structure of its components and the maintenance of proteostasis, BP.TT
19/09778-0 - THE CHAPEROME: STUDY OF THE RELATIONSHIP OF THE STRUCTURE OF ITS COMPONENTS AND THE MAINTENANCE OF PROTEOSTASIS, BP.TT - associated scholarships

Abstract

One of the most interesting challenges in science is the understanding of the structure/function relationship of proteins because these macromolecules are involved in virtually all cellular physiological functions. Accordingly, this knowledge can have several applications, including the production of proteins with specific functions and defined biotechnological applications. As the loss of the structure also leads to loss of function and to a high degree of cellular damage, there is also medicinal interest in this knowledge since it can generate strategies for therapeutic interventions with broad applications such as aging, stress, neurodegenerative diseases and tumor. The research groups gathered around this proposal have a high interest in the understanding of protein folding and the structure/function relationship of proteins. This research proposal focuses on the study of the chaperome, a cellular network aimed at the maintenance of homeostasis, which includes aiding the folding of several proteins, preventing unfolding in stress situations and promoting the recovery and degradation of protein aggregates. Additionally, the components of the chaperome are involved in several other complementary functions, among which the most important are maintenance of proteostasis in stress situations, signaling, phenotype stabilization, mitochondria biogenesis, immunity, preventing amyloidogenesis, etc. Our proposal aims at the production and characterization of the components of the chaperome and the investigation of the interaction between them and with client proteins. The proposal is divided between challenging but high-attainable goals and high-risk/high-gain objectives that will enable us to advance the frontier of knowledge in the area. Previous results have shown that different organisms have certain particularities in the structure/function relationship of the chaperome (for instance, the number and diversity of co-chaperones increases with organism complexity), showing that it is crucial to study the system of several species to obtain information on the functioning of this system. The same reasoning can be extrapolated to organelles since each one has its own set of chaperones/Hsps. Therefore, we chose highly relevant targets for global science and potential applications in Brazil: human being, sugarcane, Aedes aegypti, Leishmania sp, Plasmodium falciparum and yeast; cytoplasmic and mitochondrial. Therefore, this proposal has great potential to generate relevant knowledge both in the medical field, by generating strategies aimed at therapeutic intervention, and in biotechnology, by generating innovative processes in plants and microorganisms aiming to produce potential biotechnological tools. (AU)

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Scientific publications (20)
(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)
SILVA, NOELI S. M.; BERTOLINO-REIS, DAYANE E.; DORES-SILVA, PAULO R.; ANNETA, FATIMA B.; SERAPHIM, THIAGO V.; BARBOSA, LEANDRO R. S.; BORGES, JULIO C.. Structural studies of the Hsp70/Hsp90 organizing protein of Plasmodium falciparum and its modulation of Hsp70 and Hsp90 ATPase activities. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, v. 1868, n. 1, . (17/26131-5, 14/07206-6, 11/23110-0, 12/50161-8, 17/07335-9)
GONCALVES, CONRADO C.; SHARON, ITAI; SCHMEING, T. MARTIN; RAMOS, I, CARLOS H.; YOUNG, JASON C.. The chaperone HSPB1 prepares protein aggregates for resolubilization by HSP70. SCIENTIFIC REPORTS, v. 11, n. 1, . (17/26131-5, 16/03764-0)
ARAUJO, SARA A.; MARTINS, GUSTAVO H.; QUEL, NATALIA G.; ARAGAO, ANNELIZE Z. B.; MOREA, EDNA G. O.; BORGES, JULIO C.; HOURY, WALID A.; CANO, MARIA I. N.; RAMOS, I, CARLOS H.. Purification and characterization of a novel and conserved TPR-domain protein that binds both Hsp90 and Hsp70 and is expressed in all developmental stages of Leishmania major. Biochimie, v. 182, p. 51-60, . (14/25967-4, 12/50161-8, 19/11496-3, 18/04375-2, 17/26131-5)
MAIMONI CAMPANELLA, JONATAS ERICK; RAMOS JUNIOR, SERGIO LUIZ; RODRIGUES KIRALY, VANESSA THOMAZ; SEVERO GOMES, ANTONIEL AUGUSTO; DE BARROS, ANDREA COELHO; MATEOS, PABLO ACERA; FREITAS, FERNANDA ZANOLLI; DE MATTOS FONTES, MARCOS ROBERTO; BORGES, JULIO CESAR; BERTOLINI, MARIA CELIA. Biochemical and biophysical characterization of the RVB-1/RVB-2 protein complex, the RuvBL/RVB homologues in Neurospora crassa. Biochimie, v. 191, p. 11-26, . (17/26131-5, 08/57566-8)
SERAPHIM, V, THIAGO; NANO, NARDIN; CHEUNG, YIU WING SUNNY; ALUKSANASUWAN, SIRIPAT; COLLETI, CAROLINA; MAO, YU-QIAN; BHANDARI, VAIBHAV; YOUNG, GAVIN; HOLL, LARISSA; PHANSE, SADHNA; et al. ssembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexe. Structure, v. 30, n. 1, p. 156+, . (17/26131-5, 12/50161-8, 15/15822-1, 16/05019-0, 16/01603-9, 12/01953-9)
DORES-SILVA, PAULO ROBERTO; RODRIGUES KIRALY, VANESSA THOMAZ; DE OLIVEIRA MORITZ, MILENE NOBREGA; BALASCO SERRAO, VITOR HUGO; SIQUEIRA DOS PASSOS, PATRICIA MARIA; SPAGNOL, VALENTINE; TEIXEIRA, FELIPE ROBERTI; GAVA, LISANDRA MARQUES; CAUVI, DAVID MARIO; INACIO RAMOS, CARLOS HENRIQUE; et al. New insights on human Hsp70-escort protein 1: Chaperone activity, interaction with liposomes, cellular localizations and HSPA's self-assemblies remodeling. International Journal of Biological Macromolecules, v. 182, p. 772-784, . (14/16646-0, 14/07206-6, 17/26131-5, 16/25798-3, 09/54216-9, 12/50161-8, 17/07879-9, 11/23110-0, 17/07335-9, 12/23730-1)
PINHEIRO, GLAUCIA M. S.; AMORIM, GISELE C.; IQBAL, ANWAR; ALMEIDA, FABIO C. L.; RAMOSA, C. H. I.. Solution NMR investigation on the structure and function of the isolated J-domain from Sis1: Evidence of transient inter-domain interactions in the full-length protein. Archives of Biochemistry and Biophysics, v. 669, p. 71-79, . (18/11948-9, 17/01074-9, 17/26131-5, 12/50161-8)
SILVA, NOELI S. M.; TORRICILLAS, MARCELA S.; MINARI, KARINE; BARBOSA, LEANDRO R. S.; SERAPHIM, V, THIAGO; BORGES, JULIO C.. Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer. Archives of Biochemistry and Biophysics, v. 690, . (14/07206-6, 17/26131-5, 11/23110-0, 17/07335-9, 12/50161-8)
DORES-SILVA, PAULO R.; CAUVI, DAVID M.; COTO, AMANDA L. S.; SILVA, NOELI S. M.; BORGES, JULIO C.; DE MAIO, ANTONIO. Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes. CELL STRESS & CHAPERONES, v. 26, n. 4, p. 671-684, . (17/26131-5, 14/16646-0, 12/50161-8, 17/07335-9, 16/22477-1)
QUEL, NATALIA G.; RODRIGUES, LUIZ FERNANDO DE C.; ARAGAO, ANNELIZE Z. B.; PINHEIRO, GLAUCIA M. S.; CAMACHO, RAFAEL P.; SOUTO, DENIO E. P.; KUBOTA, LAURO T.; BARBOSA, LEANDRO R. S.; RAMOS, CARLOS H. I.. Insights into the structure and function of the C-terminus of SGTs (small glutamine-rich TPR-containing proteins): A study of the Aedes aegypti homolog. Biochimie, v. 187, p. 131-143, . (16/05019-0, 12/01953-9, 14/25967-4, 17/26131-5, 15/15822-1)
KIRALY, VANESSA T. R.; DORES-SILVA, PAULO R.; SERRAO, VITOR H. B.; CAUVI, DAVID M.; DE MAIO, ANTONIO; BORGES, JULIO C.. Thermal aggregates of human mortalin and Hsp70-1A behave as supramolecular assemblies. International Journal of Biological Macromolecules, v. 146, p. 320-331, . (17/26131-5, 14/07206-6, 11/23110-0, 12/50161-8, 17/07335-9, 14/16646-0)
ROCHA, MARINA CAMPOS; MINARI, KARINE; FABRI, JOAO HENRIQUE TADINI MARILHANO; KERKAERT, JOSHUA D.; GAVA, LISANDRA MARQUES; DA CUNHA, ANDERSON FERREIRA; CRAMER, ROBERT A.; BORGES, JULIO CESAR; MALAVAZI, IRAN. Aspergillus fumigatusHsp90 interacts with the main components of the cell wall integrity pathway and cooperates in heat shock and cell wall stress adaptation. Cellular Microbiology, v. 23, n. 2, . (16/07870-9, 15/17541-0, 17/19694-3, 17/26131-5, 17/07335-9, 14/07206-6)
DE JESUS, JEMMYSON ROMARIO; BARBOSA ARAGAO, ANNELIZE ZAMBON; ZEZZI ARRUDA, MARCO AURELIO; RAMOS, I, CARLOS H.. Optimization of a Methodology for Quantification and Removal of Zinc Gives Insights Into the Effect of This Metal on the Stability and Function of the Zinc-Binding Co-chaperone Ydj1. FRONTIERS IN CHEMISTRY, v. 7, . (17/26131-5, 12/50161-8, 18/00768-0)
DORES-SILVA, PAULO ROBERTO; CAUVI, DAVID M.; COTO, AMANDA L. S.; KIRALY, VANESSA T. R.; BORGES, JULIO C.; DE MAIO, ANTONIO. Interaction of HSPA5 (Grp78, BIP) with negatively charged phospholipid membranes via oligomerization involving the N-terminal end domain. CELL STRESS & CHAPERONES, v. 25, n. 6, . (17/26131-5, 17/07335-9, 16/22477-1, 14/16646-0, 12/50161-8)
SOUTO, DENIO E. P.; VOLPE, JAQUELINE; GONCALVES, CONRADO DE C.; RAMOS, I, CARLOS H.; KUBOTA, LAURO T.. A brief review on the strategy of developing SPR-based biosensors for application to the diagnosis of neglected tropical diseases. Talanta, v. 205, . (17/26131-5, 14/50867-3, 13/22127-2, 17/26058-6)
BATISTA, FERNANDA A. H.; RAMOS, JR., SERGIO L.; TASSONE, GIUSY; LEITAO, ANDREI; MONTANARI, CARLOS A.; BOTTA, MAURIZIO; MORI, MATTIA; BORGES, JULIO C.. Discovery of small molecule inhibitors of Leishmania braziliensis Hsp90 chaperone. Journal of Enzyme Inhibition and Medicinal Chemistry, v. 35, n. 1, p. 639-649, . (13/10712-8, 17/26131-5, 14/07206-6, 11/23110-0, 13/18009-4, 12/50161-8, 17/07335-9)
QUEL, NATALIA G.; PINHEIRO, GLAUCIA M. S.; RODRIGUES, LUIZ FERNANDO DE C.; BARBOSA, LEANDRO R. S.; HOURY, WALID A.; RAMOS, I, CARLOS H.. Heat shock protein 90 kDa (Hsp90) from Aedes aegypti has an open conformation and is expressed under heat stress. International Journal of Biological Macromolecules, v. 156, p. 522-530, . (17/26131-5, 16/05019-0, 15/15822-1, 14/25967-4, 12/01953-9)
MELO SILVA, NOELI SOARES; DE CAMARGO RODRIGUES, LUIZ FERNANDO; DORES-SILVA, PAULO ROBERTO; MONTANARI, CARLOS ALBERTO; INACIO RAMOS, CARLOS HENRIQUE; SOUZA BARBOSA, LEANDRO RAMOS; BORGES, JULIO CESAR. Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70). BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, v. 1869, n. 12, . (17/07335-9, 11/23110-0, 17/26131-5, 12/50161-8, 15/15822-1, 14/07206-6, 14/16646-0)
RAMOS, I, CARLOS H.; AYINDE, KEHINDE S.. Are Hsp90 Inhibitors Good Candidates Against Covid-19?. CURRENT PROTEIN & PEPTIDE SCIENCE, v. 22, n. 3, p. 192-200, . (17/26131-5)
FREITAS, FREDERICO CAMPOS; BORGES FERREIRA, PAULO HENRIQUE; FAVARO, DENIZE CRISTINA; DE OLIVEIRA, RONALDO JUNIO. Shedding Light on the Inhibitory Mechanisms of SARS-CoV-1/CoV-2 Spike Proteins by ACE2-Designed Peptides. JOURNAL OF CHEMICAL INFORMATION AND MODELING, v. 61, n. 3, p. 1226-1243, . (17/22822-3, 17/26131-5)

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