Next Article in Journal
Three Ecological Models to Evaluate the Effectiveness of Trichoderma spp. for Suppressing Aflatoxigenic Aspergillus flavus and Aspergillus parasiticus
Next Article in Special Issue
DNA Repair and Mutagenesis of ADP-Ribosylated DNA by Pierisin
Previous Article in Journal
A Glycoprotein-Based Surface-Enhanced Raman Spectroscopy–Lateral Flow Assay Method for Abrin and Ricin Detection
Previous Article in Special Issue
Pierisin, Cytotoxic and Apoptosis-Inducing DNA ADP-Ribosylating Protein in Cabbage Butterfly
 
 
Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
Journals
Toxins
Volume 16
Issue 7
10.3390/toxins16070313
toxins-logo
Submit to this Journal Review for this Journal Propose a Special Issue
► Article Menu

Article Menu

share Share announcement Help format_quote Cite question_answer Discuss in SciProfiles
first_page
settings
Order Article Reprints
Font Type:
Arial Georgia Verdana
Font Size:
Aa Aa Aa
Line Spacing:
Column Width:
Background:
Review

General ADP-Ribosylation Mechanism Based on the Structure of ADP-Ribosyltransferase–Substrate Complexes

by
Hideaki Tsuge
1,*,
Noriyuki Habuka
1 and
Toru Yoshida
2
1
Faculty of Life Sciences, Kyoto Sangyo University, Kyoto 6038555, Japan
2
Faculty of Sciences, Japan Women’s University, Tokyo 1120015, Japan
*
Author to whom correspondence should be addressed.
Toxins 2024, 16(7), 313; https://doi.org/10.3390/toxins16070313
Submission received: 5 June 2024 / Revised: 6 July 2024 / Accepted: 9 July 2024 / Published: 11 July 2024
(This article belongs to the Special Issue ADP-Ribosylation and Beyond)
Browse Figures
Review Reports Versions Notes

Abstract

ADP-ribosylation is a ubiquitous modification of proteins and other targets, such as nucleic acids, that regulates various cellular functions in all kingdoms of life. Furthermore, these ADP-ribosyltransferases (ARTs) modify a variety of substrates and atoms. It has been almost 60 years since ADP-ribosylation was discovered. Various ART structures have been revealed with cofactors (NAD+ or NAD+ analog). However, we still do not know the molecular mechanisms of ART. It needs to be better understood how ART specifies the target amino acids or bases. For this purpose, more information is needed about the tripartite complex structures of ART, the cofactors, and the substrates. The tripartite complex is essential to understand the mechanism of ADP-ribosyltransferase. This review updates the general ADP-ribosylation mechanism based on ART tripartite complex structures.
Keywords: ADP-ribosylation; ADP-ribosyltransferase; complex; substrate recognition ADP-ribosylation; ADP-ribosyltransferase; complex; substrate recognition

Share and Cite

MDPI and ACS Style

Tsuge, H.; Habuka, N.; Yoshida, T. General ADP-Ribosylation Mechanism Based on the Structure of ADP-Ribosyltransferase–Substrate Complexes. Toxins 2024, 16, 313. https://doi.org/10.3390/toxins16070313

AMA Style

Tsuge H, Habuka N, Yoshida T. General ADP-Ribosylation Mechanism Based on the Structure of ADP-Ribosyltransferase–Substrate Complexes. Toxins. 2024; 16(7):313. https://doi.org/10.3390/toxins16070313

Chicago/Turabian Style

Tsuge, Hideaki, Noriyuki Habuka, and Toru Yoshida. 2024. "General ADP-Ribosylation Mechanism Based on the Structure of ADP-Ribosyltransferase–Substrate Complexes" Toxins 16, no. 7: 313. https://doi.org/10.3390/toxins16070313

APA Style

Tsuge, H., Habuka, N., & Yoshida, T. (2024). General ADP-Ribosylation Mechanism Based on the Structure of ADP-Ribosyltransferase–Substrate Complexes. Toxins, 16(7), 313. https://doi.org/10.3390/toxins16070313

Note that from the first issue of 2016, this journal uses article numbers instead of page numbers. See further details here.

Article Metrics

Back to TopTop