Protein Termini Part B
- 1st Edition, Volume 719 - September 15, 2025
- Editors: David Christianson, Thomas Arnesen, Karen N. Allen
- Language: English
- Hardback ISBN:9 7 8 - 0 - 4 4 3 - 4 7 1 9 2 - 6
- eBook ISBN:9 7 8 - 0 - 4 4 3 - 4 7 1 9 3 - 3
Protein termini represent a major route to protein regulation. From the moment the very first amino acid of a polypeptide chain exits the ribosome there is potential for steering… Read more
Protein termini represent a major route to protein regulation. From the moment the very first amino acid of a polypeptide chain exits the ribosome there is potential for steering from the cellular environment. This volume of Methods in Enzymology Modifications and Targeting of Protein Termini focuses on Protein N-termini and C-termini and their modifications which include acetylation, arginylation, myristoylation and oxidation. Also, the impact of terminal modifications is covered, in particular the impact on protein turnover and the ubiquitin E3 ligases which specifically recognize protein N-termini (N-degrons) and C-termini (C-degrons). In addition to the detailed methods and laboratory protocols, the chapters include informative overviews and reviews of the different subfields.
- Provides the authority and expertise of leading contributors from an international board of authors
- Includes the latest information on modifications and targeting of proteins via their N- and C-terminal ends
Chemists, Biochemists, Molecular Biologists, and Cell Biologists with an interest in proteins and how they are modified and regulated
1. Proteome analysis of puromycin-labeled nascent polypeptides
Koshi Imami
2. HUNTER-DIA: An updated protocol for enrichment and mass spectrometry-based identification of protein N-termini
Pitter F. Huesgen
3. TERMINER - Bioinformatic detection and annotation of proteolytic protein termini in shotgun proteomics data
Oliver Schilling
4. Degronopedia: A practical guide to identifying and targeting protein degrons
Wojciech Pokrzywa
5. Quantitative Insights into Protein Turnover and Ubiquitination with HiBiT and NanoBRET
Wojciech Pokrzywa
6. Development of a flow cytometric method to evaluate the impact of N-terminal sequences on protein stability
Aditya M. Kunjapur
7. Generation and characterization of engineered N-degrons of the N-degron pathway using the ubiquitin-reference technique
Chang Hoon Ji
8. Characterization of the autophagic N-degron pathway and monitoring its chemical modulation for therapeutic development
Yong Tae Kwon
9. Characterization of the E3 ligase KCMF1 as a ZZ/N-recognin of the autophagic Arg/N-degron pathway
Chang Hoon Ji
10. Identification of Ac/N-degron-recognition domain within the MARCHF6 E3 ubiquitin ligase
Cheol-Sang Hwang
11. Affinity purification-mass spectrometry to identify nuclear protein interactions of N-terminal acetyltransferase NAA40
Antonis Kirmizis
12. TurboID technique for proximity labelling of interacting proteins
Greta Jarck
13. Chemical proteomic approaches to investigate S-prenylation
Edward W. Tate
14. Quantitative analysis of C-terminal prenylated protein levels using tandem mass tagging
Mark Distefano
15. Optimizing purification and FP-based binding assays for the E3 ligase FEM1C
Rong Huang
Koshi Imami
2. HUNTER-DIA: An updated protocol for enrichment and mass spectrometry-based identification of protein N-termini
Pitter F. Huesgen
3. TERMINER - Bioinformatic detection and annotation of proteolytic protein termini in shotgun proteomics data
Oliver Schilling
4. Degronopedia: A practical guide to identifying and targeting protein degrons
Wojciech Pokrzywa
5. Quantitative Insights into Protein Turnover and Ubiquitination with HiBiT and NanoBRET
Wojciech Pokrzywa
6. Development of a flow cytometric method to evaluate the impact of N-terminal sequences on protein stability
Aditya M. Kunjapur
7. Generation and characterization of engineered N-degrons of the N-degron pathway using the ubiquitin-reference technique
Chang Hoon Ji
8. Characterization of the autophagic N-degron pathway and monitoring its chemical modulation for therapeutic development
Yong Tae Kwon
9. Characterization of the E3 ligase KCMF1 as a ZZ/N-recognin of the autophagic Arg/N-degron pathway
Chang Hoon Ji
10. Identification of Ac/N-degron-recognition domain within the MARCHF6 E3 ubiquitin ligase
Cheol-Sang Hwang
11. Affinity purification-mass spectrometry to identify nuclear protein interactions of N-terminal acetyltransferase NAA40
Antonis Kirmizis
12. TurboID technique for proximity labelling of interacting proteins
Greta Jarck
13. Chemical proteomic approaches to investigate S-prenylation
Edward W. Tate
14. Quantitative analysis of C-terminal prenylated protein levels using tandem mass tagging
Mark Distefano
15. Optimizing purification and FP-based binding assays for the E3 ligase FEM1C
Rong Huang
- Edition: 1
- Volume: 719
- Published: September 15, 2025
- Language: English
DC
David Christianson
After completing studies for the A.B., A.M., and Ph.D. degrees in chemistry at Harvard University, David W. Christianson joined the faculty of the University of Pennsylvania, where he is currently the Roy and Diana Vagelos Professor in Chemistry and Chemical Biology. At Penn, Christianson’s research focuses on the structural and chemical biology of the zinc-dependent histone deacetylases as well as enzymes of terpene biosynthesis. His research accomplishments have been recognized by several awards, including the Pfizer Award in Enzyme Chemistry and the Repligen Award in Chemistry of Biological Processes from the American Chemical Society, a Guggenheim Fellowship, and the Elizabeth S. and Richard M. Cashin Fellowship from the Radcliffe Institute for Advanced Study at Harvard University. Christianson is also a dedicated classroom teacher, and his accomplishments in this regard have been recognized by the Lindback Award for Distinguished Teaching at Penn and a Rhodes Trust Inspirational Educator Award from Oxford University. Christianson has also held visiting professorships in the Department of Biochemistry at Cambridge University and the Department of Chemistry and Chemical Biology at Harvard University. Christianson has served with Prof. Anna Pyle as Co-Editor-in-Chief of Methods in Enzymology since 2015.
Affiliations and expertise
University of Pennsylvania, USATA
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, NorwayKA
Karen N. Allen
Dr. Karen N. Allen works at the Department of Chemistry of the Boston University, the Metcalf Center for Science and Engineering
Affiliations and expertise
Department of Chemistry, Metcalf Center for Science and Engineering, Boston University, Boston, MA, USA