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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 |
Appears in Collections: | Staff Publications Elements |
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