Review
Structure and function of the bacterial AAA protease FtsH

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Abstract

Proteolysis of regulatory proteins or key enzymes of biosynthetic pathways is a universal mechanism to rapidly adjust the cellular proteome to particular environmental needs. Among the five energy-dependent AAA+ proteases in Escherichia coli, FtsH is the only essential protease. Moreover, FtsH is unique owing to its anchoring to the inner membrane. This review describes the structural and functional properties of FtsH. With regard to its role in cellular quality control and regulatory circuits, cytoplasmic and membrane substrates of the FtsH protease are depicted and mechanisms of FtsH-dependent proteolysis are discussed. This article is part of a Special Issue entitled: AAA ATPases: structure and function.

Highlights

► FtsH is a conserved AAA protease found in eubacteria, mitochondria and chloroplasts. ► As typical for AAA+ proteases, bacterial FtsH forms barrel-shaped homo-hexamers. ► FtsH is membrane-anchored and crucial for membrane protein quality control. ► In E. coli, FtsH is essential due to regulation of lipopolysaccharide biosynthesis. ► FtsH plays a role in regulation of the E. coli heat shock response.

Abbreviations

TM
transmembrane domain
HS
heat shock
LPS
lipopolysaccharides
PL
phospholipids
PS
photosystem

Keywords

FtsH
Proteolysis
AAA protein
LpxC
LPS biosynthesis
Heat shock

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This article is part of a Special Issue entitled: AAA ATPases: structure and function.