Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0140619
Title: Acetylome analysis identifies SIRT1 targets in mRNA-processing and chromatin-remodeling in mouse liver
Authors: Kim S.-Y.
Sim C.K.
Tang H.
Han W. 
Zhang K.
Xu F. 
Keywords: BAF170 protein
binding protein
heterogeneous nuclear ribonucleoprotein C1
heterogeneous nuclear ribonucleoprotein C2
heterogeneous nuclear ribonucleoprotein L
RNA binding protein 10
SART1 protein
sirtuin 1
unclassified drug
lysine
messenger RNA
Sirt1 protein, mouse
sirtuin 1
animal tissue
Article
chromatin assembly and disassembly
controlled study
deacetylation
knockout mouse
liver
lysine acetylation
mouse
nonhuman
protein processing
RNA processing
acetylation
animal
chromatin assembly and disassembly
gene expression regulation
gene silencing
genetics
liver
metabolism
Acetylation
Animals
Chromatin Assembly and Disassembly
Gene Expression Regulation
Gene Knockdown Techniques
Liver
Lysine
Mice
RNA Processing, Post-Transcriptional
RNA, Messenger
Sirtuin 1
Issue Date: 2015
Citation: Kim S.-Y., Sim C.K., Tang H., Han W., Zhang K., Xu F. (2015). Acetylome analysis identifies SIRT1 targets in mRNA-processing and chromatin-remodeling in mouse liver. PLoS ONE 10 (10) : e0140619. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0140619
Rights: Attribution 4.0 International
Abstract: Lysine acetylation is a post-translational modification found on numerous proteins, a strategy used in cell signaling to change protein activity in response to internal or external cues. Sirtuin 1 (SIRT1) is a central lysine deacetylase involved in a variety of cellular processes including metabolism, apoptosis, and DNA repair. Here we characterize the lysine acetylome in mouse liver, and by using a model of Sirt1-/-knockout mouse, show that SIRT1 regulates the deacetylation of 70 proteins in the liver in-vivo. Amongst these SIRT1-regulated proteins, we find that four RNA-processing proteins and a chromatin-remodeling protein can be deacetylated by SIRT1 directly in-vitro. The discovery that SIRT1 has a potential role in RNA-processing suggests a new layer of regulation in the variety of functions performed by SIRT1. � 2015 Kim et al.
Source Title: PLoS ONE
URI: https://scholarbank.nus.edu.sg/handle/10635/161608
ISSN: 19326203
DOI: 10.1371/journal.pone.0140619
Rights: Attribution 4.0 International
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