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Structure and function of the bacterial AAA protease FtsH

Journal

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2011.08.015

Keywords

FtsH; Proteolysis; AAA protein; LpxC; LPS biosynthesis; Heat shock

Funding

  1. German Research Foundation (DFG) [SFB 642]
  2. Swiss National Science Foundation [31-67253.01, 3100A0-108262, 31003A-120174]

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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. (C) 2011 Elsevier B.V. All rights reserved.

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