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STRATEGIES FOR SUBSTRATE RECOGNITION BY THE AAA+ UNFOLDASES AND PROTEASES
Author(s) -
Baker Tania A.
Publication year - 2009
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.23.1_supplement.431.2
Subject(s) - proteases , signal transducing adaptor protein , protease , aaa proteins , enzyme , atpase , biochemistry , microbiology and biotechnology , peptide , biology , chemistry , signal transduction
ClpX and ClpA are AAA+ ATPases that specifically recognize and then actively unfold protein substrates. Each enzymes can act alone to disassemble protein complexes, or in a complex with the ClpP peptidase to form an ATP‐dependent protease. We are focusing on elucidating mechanisms used by these enzymes to select their substrate proteins. Some proteins are recognized via short peptide tags that bind directly to the enzyme's pore, whereas other proteins are recognized initially by interacting with the distinct peptide‐binding sites in the N‐terminal domains of the enzymes. Adaptor proteins also regulate the recognition of substrates by ClpX and ClpA. Structural, proteomic, and mechanistic studies are providing insight into the mechanisms of action of these adaptor proteins, as well as their biological impact.