Abstract:
:Cellular proteomes are dynamic and adjusted to permanently changing conditions by ATP-fueled proteolytic machineries. Among the five AAA+ proteases in Escherichia coli FtsH is the only essential and membrane-anchored metalloprotease. FtsH is a homohexamer that uses its ATPase domain to unfold and translocate substrates that are subsequently degraded without the need of ATP in the proteolytic chamber of the protease domain. FtsH eliminates misfolded proteins in the context of general quality control and properly folded proteins for regulatory reasons. Recent trapping approaches have revealed a number of novel FtsH substrates. This review summarizes the substrate diversity of FtsH and presents details on the surprisingly diverse recognition principles of three well-characterized substrates: LpxC, the key enzyme of lipopolysaccharide biosynthesis; RpoH, the alternative heat-shock sigma factor and YfgM, a bifunctional membrane protein implicated in periplasmic chaperone functions and cytoplasmic stress adaptation.
journal_name
Biol Chemjournal_title
Biological chemistryauthors
Bittner LM,Arends J,Narberhaus Fdoi
10.1515/hsz-2016-0302subject
Has Abstractpub_date
2017-05-01 00:00:00pages
625-635issue
5-6eissn
1431-6730issn
1437-4315pii
/j/bchm.2017.398.issue-5-6/hsz-2016-0302/hsz-2016-journal_volume
398pub_type
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