Enzymatic Aminoacylation of tRNA


Journal

Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969

Informations de publication

Date de publication:
2023
Historique:
medline: 5 4 2023
entrez: 3 4 2023
pubmed: 4 4 2023
Statut: ppublish

Résumé

This chapter describes the preparation of pre-charged Arg-tRNA that can be used in arginylation reaction. While in a typical arginylation reaction arginyl-tRNA synthetase (RARS) is normally included as a component of the reaction and continually charges tRNA during arginylation, it is sometimes necessary to separate the charging and the arginylation step, in order to perform each reaction under controlled conditions, e.g., for measuring the kinetics or determining the effect of different compounds and chemicals on the reaction. In such cases, tRNA

Identifiants

pubmed: 37010755
doi: 10.1007/978-1-0716-2942-0_14
doi:

Substances chimiques

Arginine-tRNA Ligase EC 6.1.1.19
RNA, Transfer, Arg 0
RNA, Transfer 9014-25-9
Amino Acyl-tRNA Synthetases EC 6.1.1.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

107-111

Subventions

Organisme : NIGMS NIH HHS
ID : R35 GM122505
Pays : United States
Organisme : NINDS NIH HHS
ID : R01 NS102435
Pays : United States

Informations de copyright

© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Références

Wang J, Han X, Saha, S, Xu, T, Rai, R, Zhang, F, Wolf, YI, Wolfson A, Yates JRR, III, 2 Kashina A (2011) Arginyltransferase is an ATP-Independent self-regulating enzyme that forms distinct functional complexes In Vivo. Chem Biol 2011 Jan 28; 18(1):121–130. https://doi.org/10.1016/j.chembiol.2010.10.016
Avcilar-Kucukgoze I, Gamper H, Polte C, Ignatova Z, Kraetzner R, Shtutman M, Hou YM, Dong DW, Kashina A (2020) tRNA(Arg)-derived fragments can serve as arginine donors for protein arginylation. Cell Chem Biol 27(7):839–849. e834. https://doi.org/10.1016/j.chembiol.2020.05.013
doi: 10.1016/j.chembiol.2020.05.013 pubmed: 32553119 pmcid: 7409373
Peacock JR, Walvoord RR, Chang AY, Kozlowski MC, Gamper H, Hou YM (2014) Amino acid-dependent stability of the acyl linkage in aminoacyl-tRNA. RNA 20(6):758–764. https://doi.org/10.1261/rna.044123.113
doi: 10.1261/rna.044123.113 pubmed: 24751649 pmcid: 4024630

Auteurs

Irem Avcilar-Kucukgoze (I)

Department of Biomedical Sciences, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA, USA.

Anna S Kashina (AS)

Department of Animal Biology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA, USA. akashina@upenn.edu.

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Classifications MeSH