Modifications and Targeting of Protein Termini
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Modifications and Targeting of Protein Termini, Volume 686 in the Methods in Enzymology series serial highlights new advances in the field, with this new volume presenting interesting chapters pn a variety of timely topics, including Optimizing purification and activity assays of N-terminal methyltransferase complexes, In vitro reconstitution of hierarchical steps of Arg/N-degron pathway, Identification of N-degrons and N-recognins by using peptide-pull-downs combined with quantitative proteomics, A decoupled Virotrap approach to study the interactomes of N-terminal proteoforms, Monitoring ADO-dependent proteolysis in cells using fluorescent reporter proteins, Site-specific α-N-terminal methylation on peptides through chemical and enzymatic methods, and more. Additional sections cover Monitoring the interactions between N-degrons and N-recognins of the Arg/N-degron pathway, Characterization and chemical modulation of p62/SQSTM1 as an autophagic N-recognin of the Arg/N-degron pathway, Analysis of higher plant N-degron pathway components and substrates via expression in S. cerevisiae, and so much more.
Key Features
- Provides the authority and expertise of leading contributors from an international board of authors
- Presents the latest release in the Methods in Enzymology serials
- Updated release includes the latest information on Modifications and Targeting of Protein Termini
Readership
Biochemists, biophysicists, molecular biologists, analytical chemists, and physiologists
Table of Contents
- 1. Optimizing purification and activity assays of N-terminal methyltransferase complexes
Christine Schaner Tooley, Haley Parker and John Tooley
2. In vitro reconstitution of hierarchical steps of Arg/N-degron pathway
Hyun Kyu Song and Bong Heon Kim
3. Identification of N-degrons and N-recognins by using peptide-pull-downs combined with quantitative proteomics
Franziska Müller and Tanja Bange
4. A decoupled Virotrap approach to study the interactomes of N-terminal proteoforms
Kris Gevaert, Annelies Bogaert and Tessa Van de Steene
5. Monitoring ADO-dependent proteolysis in cells using fluorescent reporter proteins
Thomas P. Keeley
6. Site-specific α-N-terminal methylation on peptides through chemical and enzymatic methods
Rong Huang and Ying Meng
7. Monitoring the interactions between N-degrons and N-recognins of the Arg/N-degron pathway
Yong Tae Kwon and Ah Jung Heo
8. Characterization and chemical modulation of p62/SQSTM1 as an autophagic N-recognin of the Arg/N-degron pathway
Yong Tae Kwon, Chang Hoon Ji, Min Ju Lee and Su Bin Kim
9. Characterization of C-degron-mediated protein degradation
Hsueh-Chi S. Yen, Chi-Wei Yeh, Wei-Chieh Huang, Shu-Yu Hsu, Ching-Yu Chu, Lo-Tung Lee and Kai-Han Lin
10. Analysis of higher plant N-degron pathway components and substrates via expression in S. cerevisiae
Andreas Bachmair, Nikola Winter, Aida Kozlic, Theresia Telser, Lilian Nehlin, Charlene Dambire and Michael J. Holdsworth
11. Deformylation of nascent chains on the ribosome
Marina V. Rodnina, Lena Bögeholz, Evan Mercier and Wolfgang Wintermeyer
12. High-throughput dissection of protein degradation signals with fluorescent timers
Anton Khmelinskii and Ka-Yiu Edwin Kong
13. Affinity isolation and biochemical characterisation of N-degron ligands using the N-recognin, ClpS
Kaye N. Truscott and David A. Dougan
14. Probing the effects of N-terminal acetylation on α-synuclein structure, aggregation and toxicity
Janet R. Kumita, Rosie Bell and Michele Vendruscolo
15. Peptide CoA conjugates for in situ proteomics profiling of acetyltransferase activities
Iris Finkemeier, Jürgen Eirich, Julia Sindlinger, Stefan Schön and Dirk Sch
Product details
- No. of pages: 412
- Language: English
- Copyright: © Academic Press 2023
- Published: August 1, 2023
- Imprint: Academic Press
- Hardcover ISBN: 9780443157721
About the Serial Volume Editor
Thomas Arnesen
Professor Thomas Arnesen received his Ph.D. in molecular biology from the University of Bergen, Norway in 2006. After postdoctoral work at Haukeland University Hospital and University of Rochester Medical Center, he established his own lab at the University of Bergen in 2010. His main interest has been protein N-terminal acetylation and the responsible enzymes, the N-terminal acetyltransferases (NATs). Using Saccharomyces cerevisiae and human cell models combined with in vitro approaches his lab and collaborators have i) identified and defined the presumed complete cytosolic human NAT-machinery including NATs acting post-translationally, ii) quantitatively analysed the N-terminal acetylomes of yeast and human cells, iii) developed novel assays for NAT-profiling, iv) gained mechanistic insights of the molecular and cellular effects of N-terminal acetylation, v) contributed to the understanding of the physiological and clinical importance of NATs by revealing the links between NatA and cancer cell survival and drug sensitisation, and lately by defining genetic disorders caused by pathogenic NAT variants. The Arnesen lab also contributed to solving the first NAT-structures and developing the first potent NAT-inhibitors.
With Fred Sherman and Bogdan Polevoda, Arnesen introduced the NAA (N-alpha acetyltransferase) nomenclature of the N-terminal acetyltransferase genes and proteins, and he acts as the specialist advisor for the HUGO Gene Nomenclature Committee for these genes. Arnesen is one of the founders and council members of the International Society of Protein Termini (ISPT). He has organized several symposia on N-terminal acetylation, and in 2022 he was the head organizer of the EMBO Workshop ‘Protein Termini – From mechanism to biological impact’ in Bergen, Norway. Arnesen has co-authored more than 100 peer-reviewed publications. Today he is head of the Translational Cell Signaling and Metabolism group at the Dept. of Biomedicine, UiB, supported by the Research Council of Norway and ERC. Here his team continues the basic and translational research to understand the impact of protein N-terminal modifications.
Affiliations and Expertise
Researcher, Professor, The Department of Biomedicine, Department of Biological Sciences (BIO), Arnesen Lab, University of Bergen, Bergen, Norway
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