PIF1

Last update 08 May 2025

Basic Info

Synonyms

ATP-dependent DNA helicase PIF1, C15orf20, DNA repair and recombination helicase PIF1

+ [4]

Introduction

DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance of telomeric DNA. Inhibits telomere elongation, de novo telomere formation and telomere addition to DSBs via catalytic inhibition of telomerase. Reduces the processivity of telomerase by displacing active telomerase from DNA ends. Releases telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid that is the intermediate in the telomerase reaction. Possesses an intrinsic strand annealing activity.

100 Clinical Results associated with PIF1

100 Translational Medicine associated with PIF1

0 Patents (Medical) associated with PIF1

418

Literatures (Medical) associated with PIF1

01 Feb 2025·Journal of Integrative Plant Biology

Light signaling‐dependent regulation of plastid RNA processing in Arabidopsis

Article

Author: Wu, Chunyu ; Zhang, Chunmei ; Wu, Ziying ; Zhang, Man ; Duan, Sujuan ; Jin, Hong‐Lei ; Wang, Hong‐Bin ; Wu, Qian ; Hu, Lili ; Shi, Meihui

ABSTRACTLight is a vital environmental signal that regulates the expression of plastid genes. Plastids are crucial organelles that respond to light, but the effects of light on plastid RNA processing following transcription remain unclear. In this study, we systematically examined the influence of light exposure on plastid RNA processing, focusing on RNA splicing and RNA editing. We demonstrated that light promotes the splicing of transcripts from the plastid genes rps12, ndhA, atpF, petB, and rpl2. Additionally, light increased the editing rate of the accD transcript at nucleotide 794 (accD‐794) and the ndhF transcript at nucleotide 290 (ndhF‐290), while decreasing the editing rate of the clpP transcript at nucleotide 559 (clpP‐559). We have identified key regulators of signaling pathways, such as CONSTITUTIVELY PHOTOMORPHOGENIC 1 (COP1), ELONGATED HYPOCOTYL 5 (HY5), and PHYTOCHROME‐INTERACTING FACTORs (PIFs), as important players in the regulation of plastid RNA splicing and editing. Notably, COP1 was required for GENOMES UNCOUPLED1 (GUN1)‐dependent repression of clpP‐559 editing in the light. We showed that HY5 and PIF1 bind to the promoters of nuclear genes encoding plastid‐localized RNA processing factors in a light‐dependent manner. This study provides insight into the mechanisms underlying light‐mediated post‐transcriptional regulation of plastid gene expression.

11 Nov 2024·Nucleic Acids Research

Structure-based discovery of first inhibitors targeting the helicase activity of human PIF1

Article

Author: Roche, Didier ; Poisson, Jean-François ; Antson, Alfred A ; Brandao-Neto, Jose ; Dehghani-Tafti, Saba ; Sanders, Cyril M ; Bax, Ben ; Rodeschini, Vincent ; Helfrich, Iris ; Scommegna, Francesca R ; Wever, Mark J A ; Egea-Rodriguez, Sara

AbstractPIF1 is a conserved helicase and G4 DNA binding and unwinding enzyme, with roles in genome stability. Human PIF1 (hPIF1) is poorly understood, but its functions can become critical for tumour cell survival during oncogene-driven replication stress. Here we report the discovery, via an X-ray crystallographic fragment screen (XChem), of hPIF1 DNA binding and unwinding inhibitors. A structure was obtained with a 4-phenylthiazol-2-amine fragment bound in a pocket between helicase domains 2A and 2B, with additional contacts to Valine 258 from domain 1A. The compound makes specific interactions, notably through Leucine 548 and Alanine 551, that constrain conformational adjustments between domains 2A and 2B, previously linked to ATP hydrolysis and DNA unwinding. We next synthesized a range of related compounds and characterized their effects on hPIF1 DNA-binding and helicase activity in vitro, expanding the structure activity relationship (SAR) around the initial hit. A systematic analysis of clinical cancer databases is also presented here, supporting the notion that hPIF1 upregulation may represent a specific cancer cell vulnerability. The research demonstrates that hPIF1 is a tractable target through 4-phenylthiazol-2-amine derivatives as inhibitors of its helicase action, setting a foundation for creation of a novel class of anti-cancer therapeutics.

03 Oct 2024·The Plant Cell

PHOSPHATASE 2A dephosphorylates PHYTOCHROME-INTERACTING FACTOR3 to modulate photomorphogenesis in Arabidopsis

Article

Author: Huq, Enamul ; Gómez Jaime, Andrea Paola ; Lee, Sanghwa ; Tang, Wenqiang ; Cai, Xingbo ; Sun, Yu

AbstractThe phytochrome (phy) family of sensory photoreceptors modulates developmental programs in response to ambient light. Phys also control gene expression in part by directly interacting with the bHLH class of transcription factors, PHYTOCHROME-INTERACTING FACTORS (PIFs), and inducing their rapid phosphorylation and degradation. Several kinases have been shown to phosphorylate PIFs and promote their degradation. However, the phosphatases that dephosphorylate PIFs are less understood. In this study, we describe 4 regulatory subunits of the Arabidopsis (Arabidopsis thaliana) protein PHOSPHATASE 2A (PP2A) family (B′α, B′β, B″α, and B″β) that interact with PIF3 in yeast 2-hybrid, in vitro and in vivo assays. The pp2ab″αβ and b″αβ/b′αβ mutants display short hypocotyls, while the overexpression of the B subunits induces longer hypocotyls compared with the wild type (WT) under red light. The light-induced degradation of PIF3 is faster in the b″αβ/b′αβ quadruple mutant compared with that in the WT. Consistently, immunoprecipitated PP2A A and B subunits directly dephosphorylate PIF3-MYC in vitro. An RNA-sequencing analysis shows that B″α and B″β alter global gene expression in response to red light. PIFs (PIF1, PIF3, PIF4, and PIF5) are epistatic to these B subunits in regulating hypocotyl elongation under red light. Collectively, these data show an essential function of PP2A in dephosphorylating PIF3 to modulate photomorphogenesis in Arabidopsis.

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PIF1

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