scholarly journals The KRAB Zinc Finger Protein Roma/Zfp157 Is a Critical Regulator of Cell-Cycle Progression and Genomic Stability

Cell Reports ◽  
2016 ◽  
Vol 15 (4) ◽  
pp. 724-734 ◽  
Author(s):  
Teresa L.F. Ho ◽  
Guillaume Guilbaud ◽  
J. Julian Blow ◽  
Julian E. Sale ◽  
Christine J. Watson
eLife ◽  
2016 ◽  
Vol 5 ◽  
Author(s):  
Johann Mignolet ◽  
Seamus Holden ◽  
Matthieu Bergé ◽  
Gaël Panis ◽  
Ezgi Eroglu ◽  
...  

Protein polarization underlies differentiation in metazoans and in bacteria. How symmetric polarization can instate functional asymmetry remains elusive. Here, we show by super-resolution photo-activated localization microscopy and edgetic mutations that the bitopic zinc-finger protein ZitP implements specialized developmental functions – pilus biogenesis and multifactorial swarming motility – while shaping distinct nanoscale (bi)polar architectures in the asymmetric model bacterium Caulobacter crescentus. Polar assemblage and accumulation of ZitP and its effector protein CpaM are orchestrated in time and space by conserved components of the cell cycle circuitry that coordinate polar morphogenesis with cell cycle progression, and also act on the master cell cycle regulator CtrA. Thus, this novel class of potentially widespread multifunctional polarity regulators is deeply embedded in the cell cycle circuitry.


2018 ◽  
Vol 46 (5) ◽  
pp. 2459-2478 ◽  
Author(s):  
David Dilworth ◽  
Geoff Gudavicius ◽  
Xiaoxue Xu ◽  
Andrew K J Boyce ◽  
Connor O’Sullivan ◽  
...  

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Urvi Thacker ◽  
Tekle Pauzaite ◽  
James Tollitt ◽  
Maria Twardowska ◽  
Charlotte Harrison ◽  
...  

Abstract CIP1-interacting zinc finger protein 1 (CIZ1) is a nuclear matrix associated protein that facilitates a number of nuclear functions including initiation of DNA replication, epigenetic maintenance and associates with the inactive X-chromosome. Here, to gain more insight into the protein networks that underpin this diverse functionality, molecular panning and mass spectrometry are used to identify protein interaction partners of CIZ1, and CIZ1 replication domain (CIZ1-RD). STRING analysis of CIZ1 interaction partners identified 2 functional clusters: ribosomal subunits and nucleolar proteins including the DEAD box helicases, DHX9, DDX5 and DDX17. DHX9 shares common functions with CIZ1, including interaction with XIST long-non-coding RNA, epigenetic maintenance and regulation of DNA replication. Functional characterisation of the CIZ1-DHX9 complex showed that CIZ1-DHX9 interact in vitro and dynamically colocalise within the nucleolus from early to mid S-phase. CIZ1-DHX9 nucleolar colocalisation is dependent upon RNA polymerase I activity and is abolished by depletion of DHX9. In addition, depletion of DHX9 reduced cell cycle progression from G1 to S-phase in mouse fibroblasts. The data suggest that DHX9-CIZ1 are required for efficient cell cycle progression at the G1/S transition and that nucleolar recruitment is integral to their mechanism of action.


2016 ◽  
Vol 101 (3) ◽  
pp. 367-380 ◽  
Author(s):  
Samuel Bru ◽  
Joan Marc Martínez-Laínez ◽  
Sara Hernández-Ortega ◽  
Eva Quandt ◽  
Javier Torres-Torronteras ◽  
...  

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