The proteasome complex is a broad spectrum protease present in all eukaryotes, which functions to carry out selective, efficient and progressive hydrolysis of intracellular target proteins. The proteasome plays a prominent role in the control of a diverse array of basic cellular processes by rapidly catalyzing numerous biological reactions.
The proteasome complex is composed of a 20S catalytic core and one or two terminal 19S regulatory units. The 20S catalytic domain is barrel-shaped and consists of seven structurally similar α- and β-subunits. In the inactive state, the external α-subunits act as a physical barrier to prevent peptide substrates accessing the active site on the β-subunits. The 19S regulatory units recognize proteins marked by polyubiquitin chains, remove the chain, entrap the protein moiety and open the 20S α-subunits allowing the β-subunits to degrade the protein. Assembly of the 20S domain is very complex and requires extrinsic (eg PAC1) and intrinsic (eg C-tail of β-subunits) chaperones. The assembly mechanism of the 19S domain is poorly understood, but Hsp90 is thought to play a role.
Regulation of the proteasome complex is mediated by proteasome interacting proteins (PIPs). There are two classes of PIPs; protein factors related to the ubiquitylation system such as the deubiquitylating enzyme, Usp14 and auxillary factors that regulate proteasome functions via direct binding, for example Ecm29.View all products for Proteasome »
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Literature for Proteasome
Cancer Research Guide
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