FtsH Protease-Mediated Regulation of Various Cellular Functions
FtsH, a member of the AAA (ATPases associated with a variety of cellular activities) family of proteins, is an ATP-dependent protease of ∼71 kDa anchored to the inner membrane. It plays crucial roles in a variety of cellular processes. It is responsible f
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FtsH Protease-Mediated Regulation of Various Cellular Functions Takashi Okuno and Teru Ogura
Abstract FtsH, a member of the AAA (ATPases associated with a variety of cellular activities) family of proteins, is an ATP-dependent protease of ~71 kDa anchored to the inner membrane. It plays crucial roles in a variety of cellular processes. It is responsible for the degradation of both membrane and cytoplasmic substrate proteins. Substrate proteins are unfolded and translocated through the central pore of the ATPase domain into the proteolytic chamber, where the polypeptide chains are processively degraded into short peptides. FtsH is not only involved in the proteolytic elimination of unnecessary proteins, but also in the proteolytic regulation of a number of cellular functions. Its role in proteolytic regulation is achieved by one of two approaches, either the cellular levels of a regulatory protein are controlled by processive degradation of the entire protein, or the activity of a particular substrate protein is modified by processing. In the latter case, protein processing requires the presence of a stable domain within the substrate. Since FtsH does not have a robust unfolding activity, this stable domain is sufficient to abort processive degradation of the protein – resulting in release of a stable protein fragment. Keywords FtsH • Processive degradation • Protein processing • Protein quality control • Regulation of lipid synthesis
T. Okuno Department of Material and Biological Chemistry, Faculty of Science, Yamagata University, Yamagata 990-8560, Japan e-mail: [email protected] T. Ogura (*) Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860-0811, Japan e-mail: [email protected] D.A. Dougan (ed.), Regulated Proteolysis in Microorganisms, Subcellular Biochemistry 66, DOI 10.1007/978-94-007-5940-4_3, © Springer Science+Business Media Dordrecht 2013
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T. Okuno and T. Ogura
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Fig. 3.1 Various cellular functions regulated by FtsH protease. FtsH, a membrane-bound AAA protease, is responsible for regulation of various cellular functions in E. coli. FtsH acts on both membrane and cytoplasmic substrate proteins. FtsH functions not only in the proteolytic elimination of unnecessary proteins but also controls the cellular levels of several regulatory proteins and the processing of specific substrate proteins (For further details refer to the main text)
Introduction FtsH is an evolutionarily conserved protein that is present in all bacterial cells. It consists of transmembrane segment 1 (TM1), periplasmic domain, TM2, cytoplasmic ATPase and protease domains in this order from the N-terminus [1–6]. FtsH is a zinc-binding metalloprotease, which forms a homohexameric ring-shaped structure. It can degrade unstructu
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