https://scholars.lib.ntu.edu.tw/handle/123456789/606024
Title: | Expanding the Substrate Specificity of Macro Domains toward 3″-Isomer of O-Acetyl-ADP-ribose | Authors: | Chiu Y.-C Tseng M.-C CHUN-HUA HSU |
Keywords: | 3?-O-acetyl-ADP-ribose;crystal structure;deacetylase;macro domain;Poa1p;Cell signaling;Isomers;Nucleotides;Physiological models;Active site residues;Deacetylase activity;Intracellular signaling;Nucleotide metabolism;Physiological roles;Structural characterization;Structural insights;Substrate specificity;Yeast | Issue Date: | 2021 | Journal Volume: | 11 | Journal Issue: | 17 | Start page/Pages: | 11075-11090 | Source: | ACS Catalysis | Abstract: | O-Acetyl-ADP-ribose (OAADPR) is a signaling molecule identified from the conserved sirtuin reaction inSaccharomyces cerevisiae, involved in the important cellular functions of gene silencing, redox regulation, and aging. Here, we performed biochemical and structural characterization of the yeast Poa1p macro domain in detail, uncovering an unusual deacetylase activity favoring 3?- and 1?-isomers ofO-acetyl-ADP-ribose. The unique active-site residues of Poa1p contributing to the distinct substrate specificity thus shed light on the divergent branch of a POA1-like subclass. Moreover, disruption of Poa1p expression in yeast showed a striking sensitivity to transcriptional stress, which implies a physiological role in response to nucleotide depletion. These findings provide biochemical and structural insights into a noncanonical 3?-O-acetyl-ADP-ribose deacetylase, which plays a critical role in cellular nucleotide metabolism for intracellular signaling and the regulatory process. ? 2021 American Chemical Society |
URI: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85114431772&doi=10.1021%2facscatal.1c01943&partnerID=40&md5=9737f01aa13cd691f493dcea89bbb0b2 https://scholars.lib.ntu.edu.tw/handle/123456789/606024 |
ISSN: | 21555435 | DOI: | 10.1021/acscatal.1c01943 |
Appears in Collections: | 農業化學系 |
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