Ontology type: schema:ScholarlyArticle
2010-12
AUTHORSRaffaella Pierleoni, Michele Menotta, Antonella Antonelli, Carla Sfara, Giordano Serafini, Sabrina Dominici, Maria Elena Laguardia, Annalisa Salis, Gianluca Damonte, Lucia Banci, Marco Porcu, Paolo Monini, Barbara Ensoli, Mauro Magnani
ABSTRACTThe redox state of the cysteine-rich region of the HIV Tat protein is known to play a crucial role in Tat biological activity. In this article, we show that Tat displays two alternative functional states depending on the presence of either one or three reduced sulphydryl groups in the cysteine-rich region, respectively. Using different approaches, a disulfide pattern has been defined for the Tat protein and a specific DTT-dependent breaking order of disulfide bonds highlighted. The Tat redox state deeply influences macrophage protein uptake. Immunoistochemistry analysis shows that the oxidized protein does not enter cells, whereas partially reduced protein reaches the cytosol and, to a limited extent, the nucleus. Finally electrophoretic analysis shows Tat high-molecular weight multi-aggregation, resulting in the loss of biological activity. This is due to strong electrostatic and metal-binding interactions, whereas Tat dimerization involves metal-binding interactions as well as disulfide bond formation. More... »
PAGES105-118
http://scigraph.springernature.com/pub.10.1007/s11010-010-0564-9
DOIhttp://dx.doi.org/10.1007/s11010-010-0564-9
DIMENSIONShttps://app.dimensions.ai/details/publication/pub.1017534425
PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/20721684
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"description": "The redox state of the cysteine-rich region of the HIV Tat protein is known to play a crucial role in Tat biological activity. In this article, we show that Tat displays two alternative functional states depending on the presence of either one or three reduced sulphydryl groups in the cysteine-rich region, respectively. Using different approaches, a disulfide pattern has been defined for the Tat protein and a specific DTT-dependent breaking order of disulfide bonds highlighted. The Tat redox state deeply influences macrophage protein uptake. Immunoistochemistry analysis shows that the oxidized protein does not enter cells, whereas partially reduced protein reaches the cytosol and, to a limited extent, the nucleus. Finally electrophoretic analysis shows Tat high-molecular weight multi-aggregation, resulting in the loss of biological activity. This is due to strong electrostatic and metal-binding interactions, whereas Tat dimerization involves metal-binding interactions as well as disulfide bond formation.",
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"name": "Effect of the redox state on HIV-1 tat protein multimerization and cell internalization and trafficking",
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