Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
4359042 | Research in Microbiology | 2009 | 11 Pages |
Abstract
Clp proteases are the most widespread energy-dependent proteases in bacteria. Their two-component architecture of protease core and ATPase rings results in an inventory of several Clp protease complexes that often coexist. Here, we present insights into Clp protease function, from their assembly to substrate recruitment and processing, and how this is coupled to the expense of energy.
Related Topics
Life Sciences
Immunology and Microbiology
Applied Microbiology and Biotechnology
Authors
Wolfgang Kress, Željka Maglica, Eilika Weber-Ban,