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| Molecular chaperones are a group of highly interactive proteins that modulate the folding and unfolding of other proteins, or the assembly and disassembly of protein-protein, protein-DNA, and protein-RNA complexes [1]. In addition, chaperones are known to be involved in many cellular processes and pathways such as protein translocation across membranes, ribosomal RNA processing, and endoplasmic reticulum associated protein degradation (ERAD). |
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Most chaperones are
members of the heat shock regulon and this seems to be a generally conserved
feature for most known molecular chaperones. Chaperones are usually categorized
into distinct groups according to their sequence similarity, which also reflects
their distinct functions. The model organism Saccharomyces cerevisiae (budding
yeast) has 63 chaperone proteins, classified into the following categories: Hsp40,
Hsp70, Hsp90, the prefoldin/GimC complex (PFD), CCT/TRiC complex (CCT),
AAA+ family, and small heat shock proteins [2].
ChaperoneDB is a comprehensive database that collects and organizes the genetic and genomics information associated with molecular chaperones. The current version (2009) is focused on chaperones in the budding yeast. Users can browse or query individual chaperones to extract proteins or substrates that have a genetic interaction or a protein-protein interaction with the chaperone [3]. For each chaperone or protein substrate, the server generates a network graph in SVG format. The database also links to external databases such as SGD and BioGrid. |
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1. Hartl F., Hayer-Hartl M., Science 2002 295(5561) 2. Zhao R. et al Cell 2005 120(5) 3. Gong Y. et al Mol Syst Biol 2009 5:275 |
