Article ID Journal Published Year Pages File Type
4359042 Research in Microbiology 2009 11 Pages PDF
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.

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Life Sciences Immunology and Microbiology Applied Microbiology and Biotechnology
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