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Sugarcane Hsp101 is a hexameric chaperone that binds nucleotides |
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| Authors: | Cagliari Thiago C da Silva Viviane C H Borges Júlio C Prando Alessandra Tasic Ljubica Ramos Carlos H I |
| Affiliation: | a Institute of Chemistry, University of Campinas-UNICAMP, P.O. Box 6154, 13083-970, Campinas, SP, Brazil b Institute of Biology, University of Campinas-UNICAMP, P.O. Box 6154, 13083-970, Campinas, SP, Brazil c Institute of Chemistry of São Carlos, University of São Paulo, São Carlos, SP, 13560-970, Brazil d Instituto Nacional de Ciência e Tecnologia em Biologia Estrutural e Bioimagem, Brazil |
| Abstract: | The Clp/Hsp100 AAA+ chaperone family is involved in recovering aggregated proteins and little is known about other orthologs of the well studied ClpB from Escherichia coli and Hsp104 from Saccharomyces cerevisiae. Plant Hsp101 is a good model for understanding the relationship between the structure and function of Hsp100 proteins and to investigate the role of these chaperones in disaggregation processes. Here, we present the cloning and purification of a sugarcane ortholog, SHsp101, which is expressed in sugarcane cells and is a folded hexamer that is capable of binding nucleotides. Thus SHsp101 has the structural and functional characteristics of the Clp/Hsp100 AAA+ family. |
| Keywords: | AUC, analytical ultracentrifugation CD, circular dichroism Hsp, heat shock protein STD-NMR, saturation transfer difference NMR |
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