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Protein Degradation: Ubiquitin and the Chemistry of Life, by Raymond J. Deshaies

By Raymond J. Deshaies

The 1st quantity in a brand new sequence devoted to protein degradation, this ebook lays the principles of special protein breakdown through the ubiquitin pathway.
the exceptional value of the ubiquitin pathway has been famous with the 2004 Nobel Prize in Chemistry for Aaaron Chiechanover, Avram Hershko, and Irwin Rose. Aaron Ciechanover is without doubt one of the editors of this series,
and Avram Hershko has contributed to the hole bankruptcy of the current volume.
Drawing at the the services of 2 Nobel prize winners, this useful reference compiles details at the preliminary steps of the ubiquitin pathway. beginning out with a vast view of protein degradation and its capabilities in mobile law, it then is going directly to study the molecular mechanisms of ubiquitin conjugation and recycling intimately. All at the moment identified periods of ubiquitin protein ligases are handled right here, together with most recent structural info on those enzymes.
additional volumes within the sequence hide the functionality of the proteasome, and the jobs of the ubiquitin pathway in regulating key mobile techniques, in addition to its pathophysiological illness states.
Required examining for molecular biologists, phone biologists and physiologists with an curiosity in protein degradation.Content:
Chapter 1 short historical past of Protein Degradation and the Ubiquitin process (pages 1–9): Avram Hershko
Chapter 2 N?terminal Ubiquitination: now not this kind of infrequent amendment (pages 10–20): Prof. Dr. Aaron Ciechanover
Chapter three Evolutionary foundation of the Activation Step in the course of Ubiquitin?dependent Protein Degradation (pages 21–43): Hermann Schindelin
Chapter four RING arms and family: Determinators of Protein destiny (pages 44–101): Kevin L. Lorick, Yien?Che Tsai, Yili Yang and Allan M. Weissman
Chapter five Ubiquitin?conjugating Enzymes (pages 102–134): Michael J. Eddins and Cecile M. Pickart
Chapter 6 The SCF Ubiquitin E3 Ligase (pages 135–155): Leigh Ann Higa and Hui Zhang
Chapter 7 The Structural Biology of Ubiquitin–Protein Ligases (pages 156–189): Ning Zheng and Nikola P. Pavletich
Chapter eight The Deubiquitinating Enzymes (pages 190–219): Nathaniel S. Russell and Keith D. Wilkinson
Chapter nine The 26S Proteasome (pages 220–247): Prof. Dr. Martin Rechsteiner
Chapter 10 Molecular Machines for Protein Degradation (pages 248–287): Matthias Bochtler, Michael Groll, Hans Brandstetter, Tim Clausen and Robert Huber
Chapter eleven Proteasome Regulator, PA700 (19S Regulatory Particle) (pages 288–316): George N. DeMartino and Cezary Wojcik
Chapter 12 Bioinformatics of Ubiquitin domain names and Their Binding companions (pages 318–347): Kay Hofmann
Chapter thirteen The COP9 Signalosome: Its attainable position within the Ubiquitin approach (pages 348–369): Dawadschargal Bech?Otschir, Barbara Kapelari and Wolfgang Dubiel

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Extra info for Protein Degradation: Ubiquitin and the Chemistry of Life, Volume 1

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Activation-dependent ubiquitination of a T cell antigen receptor subunit on multiple intracellular lysines. J. Biol. , 1994, 269, 14244–14247. , Staszewski, L. and Bohmann, D. Ubiquitin-dependent c-Jun degradation in vivo is mediated by the d-domain. Cell, 1994, 78, 787– 798. King, R. , Glotzer, M. and Kirschner, M. W. Mutagenic analysis 11 12 13 14 15 16 17 18 of the destruction signal of mitotic cyclins and structural characterization of ubiquitinated intermediates. Mol. Biol. Cell, 1996, 7, 1343–1357.

The fact that residues 182 to 188 of MoeB are disordered could indicate that they are involved in protein–protein interactions with either the rhodanese domain or the cysteine desulfurase. Cys187 of MoeB could either cleave the acyldisulfide between the cysteine of the rhodanese domain and the MoaD C-terminus as suggested by Matthies et al. [43], or could itself form an acyldisulfide bond with the MoaD C-terminus prior to formation of the MoaD thiocarboxylate. 4 Structure of the NEDD8 Activator NEDD8 (Rub1 in yeast) is a UbL, which is attached to cullins following activation by a specific E1 and transfer by an E2 enzyme [47].

Ciechanover, M. Rechsteiner Copyright 8 2005 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim ISBN: 3-527-30837-7 22 3 Evolutionary Origin of the Activation Step During Ubiquitin-dependent Protein Degradation zymes involved in Moco biosynthesis strongly suggest that the two-component systems consisting of a UbL protein and a cognate E1 enzyme, which are present exclusively in eukaryotes, are derived from the simpler and universally distributed MoaD–MoeB pair. 1 Activation of Ubiquitin and Ubiquitin-like Proteins The transfer of ubiquitin and related protein modifiers (reviewed in [1]) such as SUMO [2], NEDD8 [3], Apg12 [4], Apg8 [5], ISG15 [6], Urm1 [7] and Hub1p [8] is initiated by an activation step catalyzed by an activating (E1) enzyme, which is specific for the respective modifier [9, 10].

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