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Evolution of the role of Cdc48 and its interactions with the 20S peptidase (478.1)
Author(s) -
Sauer Robert,
Barthelme Dominik,
Grabenstatter Jon,
Jauregui Ruben,
Chen James,
Baker Tania
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.478.1
Subject(s) - proteolysis , proteasome , archaea , ring (chemistry) , ubiquitin , proteases , biochemistry , actinobacteria , atp hydrolysis , function (biology) , chemistry , aaa proteins , enzyme , biophysics , microbiology and biotechnology , biology , atpase , 16s ribosomal rna , organic chemistry , gene
Proteasomes are ubiquitous ATP‐dependent proteases that function in eukarya, archaea, and actinobacteria. These proteolytic machines employ a barrel‐shaped 20S core peptidase and a hexameric AAA+ unfolding ring that unfolds and spools substrates into the chamber of the peptidase. Interestingly, the 20S peptidase can function with two very different types of AAA+ unfolding rings. For example, archaeal 20S can combine either with the double‐ring Cdc48 unfoldase or the single‐ring PAN unfoldase to execute ATP‐dependent proteolysis. Single‐ring AAA+ unfoldases that are homologous to PAN also function with the 20S in protein degradation in eukarya (the Rpt1‐6 ring of the 26S proteasome) and actinobacteria (Mpa). We will discuss differences between single‐ring and double‐ring AAA+ unfoldases, how the interactions between the 20S peptidase and its AAA+ partner are controlled, and possible mechanisms by which the N domain of Cdc48 controls rates of ATP hydrolysis, substrate unfolding, and affinity for the 20S peptidase.