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Sirt1 carboxyl-domain is an ATP-repressible domain that is transferable to other proteins

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Title
Sirt1 carboxyl-domain is an ATP-repressible domain that is transferable to other proteins
Author(s)
Hyeog Kang; Shinichi Oka; Duck-Yeon Lee; Junhong Park; Angel M. Aponte; Young-Sang Jung; Jacob Bitterman; Peiyong Zhai; Yi He; Harned Kooshapur; Rodolfo Ghirlando; Nico Tjandra; Sean B. Lee; Myung K. Kim; Junichi Sadoshirna; Jay H. Chung
Publication Date
2017-05
Journal
NATURE COMMUNICATIONS, v.8, no., pp.15560 -
Publisher
NATURE PUBLISHING GROUP
Abstract
Sirt1 is an NADþ-dependent protein deacetylase that regulates many physiological functions, including stress resistance, adipogenesis, cell senescence and energy production. Sirt1 can be activated by energy deprivation, but the mechanism is poorly understood. Here, we report that Sirt1 is negatively regulated by ATP, which binds to the C-terminal domain (CTD) of Sirt1. ATP suppresses Sirt1 activity by impairing the CTD’s ability to bind to the deacetylase domain as well as its ability to function as the substrate recruitment site. ATP, but not NADþ, causes a conformational shift to a less compact structure. Mutations that prevent ATP binding increase Sirt1’s ability to promote stress resistance and inhibit adipogenesis under high-ATP conditions. Interestingly, the CTD can be attached to other proteins, thereby converting them into energy-regulated proteins. These discoveries provide insight into how extreme energy deprivation can impact Sirt1 activity and underscore the complex nature of Sirt1 structure and regulation. (c) The Author(s) 2017
URI
http://pr.ibs.re.kr/handle/8788114/4213
DOI
10.1038/ncomms15560
ISSN
2041-1723
Appears in Collections:
Center for Genomic Integrity(유전체 항상성 연구단) > Journal Papers (저널논문)
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