Autor(es)

Batista, Fernanda A. H. ^{[1, 2]} ; Dores-Silva, Paulo R. ^[2] ; Borges, Julio C. ^[2]

Afiliação do(s) autor(es)

^[1] CNPEM, Lab Nacl Biociencias LNBio, BR-13083970 Campinas, SP - Brazil

^[2] Univ Sao Paulo, Inst Quim Sao Carlos, POB 780, BR-13560970 Sao Carlos, SP - Brazil

• Tipo de documento: Artigo de Revisão
• Fonte: CURRENT PROTEOMICS; v. 16, n. 1, p. 12-21, 2019.
• Citações Web of Science: 0

Resumo

Molecular chaperones have several critical functions in protein metabolism. Among them, some are involved in processes that culminate in the extraction of entangled polypeptides from protein aggregates, releasing unfolded structures prone to be refolded or directed to degradation. This action avoids the effect of toxic aggregates on cells and tissues. Molecular chaperones belonging to the Hsp100 family are widely distributed from unicellular and sessile organisms up to fungi and plants, exerting key functions related to the reduction of the effects caused by different forms of stress. The Hsp100 proteins belong to the AAA+ (ATPases Associated with diverse cellular Activities) family and form multichaperone systems with Hsp70 and small Hsp chaperones families. However, Hsp100 are absent in metazoan, where protein disaggregation action is performed by a system involving the Hsp70 family, including Hsp110 and J-protein co-chaperones. Here, the structural and functional aspects of these protein disaggregation systems will be reviewed and discussed in the perspective of the Hsp100 system absent in the metazoan kingdom. This feature focuses on Hsp100 as a hot spot for drug discovery against human infectious diseases such as leishmaniasis and malaria, as Hsp100 is critical for microorganisms. The current data available for Hsp100 in Leishmania spp. and Plasmodium spp. are also reviewed. (AU)

• Processo FAPESP: 14/07206-6 - Estudos da HSP70 mitocondrial de humanos e de protozoários: abordagem estrutural e funcional
• Beneficiário: Julio Cesar Borges
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 14/16646-0 - Mortalina humana: interação com co-chaperonas, p53 e mutantes, cinética de agregação, regulação/modulação e secreção por vesículas
• Beneficiário: Paulo Roberto das Dores da Silva
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado
• Processo FAPESP: 07/05001-4 - Estudos dos sistemas chaperones moleculares HSP70 e HSP90 de parasitas
• Beneficiário: Julio Cesar Borges
• Modalidade de apoio: Auxílio à Pesquisa - Jovens Pesquisadores
• Processo FAPESP: 12/50161-8 - Estudo da estrutura e função da chaperona Hsp90 com ênfase no seu papel em homeostase celular
• Beneficiário: Carlos Henrique Inacio Ramos
• Modalidade de apoio: Auxílio à Pesquisa - Temático
• Processo FAPESP: 11/23110-0 - Uso da calorimetria de titulação isotérmica para a determinação de propriedades termodinâmicas de interação de proteína-ligante e proteína-proteína
• Beneficiário: Julio Cesar Borges
• Modalidade de apoio: Auxílio à Pesquisa - Regular