Biochemical insight into pseudouridine synthase 7 (PUS7) as a novel interactor of sirtuin, SIRT1.

Abstract

Sirtuin1 (SIRT1) forms a dynamic regulatory network with multiple proteins. The SIRT1 protein interactome comprises histone, non-histone substrates, and modulators of SIRT1 deacetylase. Proteomic studies have enlisted several proteins in SIRT1 network, but the structural and functional details of their interactions remain largely unexplored. In this study, we establish Pseudouridine synthase 7 (PUS7), a nuclear protein involved in stem cell development and intellectual disabilities, as a novel interactor of SIRT1. The binding regions are predicted and analyzed based on molecular docking studies. The direct interaction occurs between SIRT1 and PUS7, as evidenced by pull-down studies and surface plasmon resonance (SPR) assay. Furthermore, the truncation studies unambiguously suggested that the N-terminal region of PUS7 is essential for forming a stable complex with SIRT1. Overall, our results suggest that PUS7 may regulate the SIRT1 function when it directly interacts with SIRT1.

• Authors: Sayli Dalal, Prashant Deshmukh, Sruthi Unni, Sivaraman Padavattan, Balasundaram Padmanabhan
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 518 Issue 3 Pg. 598-604 (10 20 2019) ISSN: 1090-2104 [Electronic] United States
• PMID: 31451225 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: Copyright © 2019 Elsevier Inc. All rights reserved.

Chemical References

• SIRT1 protein, human
• Sirtuin 1
• Intramolecular Transferases
• PUS7 protein, human

Topics

• Binding Sites
• Humans
• Intramolecular Transferases (chemistry, metabolism)
• Kinetics
• Molecular Docking Simulation
• Protein Binding
• Protein Interaction Maps
• Sirtuin 1 (chemistry, metabolism)