Cargando…
Conserved Distal Loop Residues in the Hsp104 and ClpB Middle Domain Contact Nucleotide-binding Domain 2 and Enable Hsp70-dependent Protein Disaggregation
The homologous hexameric AAA(+) proteins, Hsp104 from yeast and ClpB from bacteria, collaborate with Hsp70 to dissolve disordered protein aggregates but employ distinct mechanisms of intersubunit collaboration. How Hsp104 and ClpB coordinate polypeptide handover with Hsp70 is not understood. Here, w...
Autores principales: | DeSantis, Morgan E., Sweeny, Elizabeth A., Snead, David, Leung, Eunice H., Go, Michelle S., Gupta, Kushol, Wendler, Petra, Shorter, James |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3887210/ https://www.ncbi.nlm.nih.gov/pubmed/24280225 http://dx.doi.org/10.1074/jbc.M113.520759 |
Ejemplares similares
-
Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation
por: Carroni, Marta, et al.
Publicado: (2014) -
Substrate Discrimination by ClpB and Hsp104
por: Johnston, Danielle M., et al.
Publicado: (2017) -
ATPase Activity and ATP-dependent Conformational Change in the Co-chaperone HSP70/HSP90-organizing Protein (HOP)
por: Yamamoto, Soh, et al.
Publicado: (2014) -
A Platform to View Huntingtin Exon 1 Aggregation Flux in the Cell Reveals Divergent Influences from Chaperones hsp40 and hsp70
por: Ormsby, Angelique R., et al.
Publicado: (2013) -
S-Glutathionylation of human inducible Hsp70 reveals a regulatory mechanism involving the C-terminal α-helical lid
Publicado: (2020)