When, how and why? Regulated proteolysis by the essential FtsH protease in Escherichia coli.

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 Chem

journal_title

Biological chemistry

authors

Bittner LM,Arends J,Narberhaus F

doi

10.1515/hsz-2016-0302

subject

Has Abstract

pub_date

2017-05-01 00:00:00

pages

625-635

issue

5-6

eissn

1431-6730

issn

1437-4315

pii

/j/bchm.2017.398.issue-5-6/hsz-2016-0302/hsz-2016-

journal_volume

398

pub_type

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