Biochemical and structural analysis of N-terminal acetyltransferases.
Animals
Catalytic Domain
Cell Line
Cloning, Molecular
/ methods
Crystallization
/ methods
Crystallography, X-Ray
/ methods
Enzyme Assays
/ methods
Escherichia coli
/ genetics
Humans
Models, Molecular
N-Terminal Acetyltransferases
/ chemistry
Protein Conformation
Recombinant Proteins
/ chemistry
Up-Regulation
Biophysical analysis
Co-translational acetylation
N-terminal acetyltransferases
NATs
Protein acetyltransferases
Protein complexes
X-ray crystallography
Journal
Methods in enzymology
ISSN: 1557-7988
Titre abrégé: Methods Enzymol
Pays: United States
ID NLM: 0212271
Informations de publication
Date de publication:
2019
2019
Historique:
entrez:
14
10
2019
pubmed:
14
10
2019
medline:
3
6
2020
Statut:
ppublish
Résumé
N-terminal acetylation is a co- and post-translational modification catalyzed by the conserved N-terminal acetyltransferase (NAT) family of enzymes. A majority of the human proteome is modified by the human NATs (NatA-F and H), which are minimally composed of a catalytic subunit and as many as two auxiliary subunits. Together, NATs specifically regulate many cellular functions by influencing protein activities such as their degradation, membrane targeting, and protein-protein interactions. This chapter will describe methods developed for their preparation, and their biochemical and structural characterization. This will include methodologies for expression and purification of recombinant NAT protein, kinetic assays, biochemical and biophysical assays, and strategies for structural studies.
Identifiants
pubmed: 31606079
pii: S0076-6879(19)30296-4
doi: 10.1016/bs.mie.2019.07.016
pmc: PMC6884420
mid: NIHMS1059602
pii:
doi:
Substances chimiques
Recombinant Proteins
0
N-Terminal Acetyltransferases
EC 2.3.1.88
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
271-299Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM118090
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM071339
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM133398
Pays : United States
Informations de copyright
© 2019 Elsevier Inc. All rights reserved.
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