Sign in to use this feature.

Years

Between: -

Subjects

remove_circle_outline
remove_circle_outline

Journals

Article Types

Countries / Regions

Search Results (1)

Search Parameters:
Keywords = HIRIP3

Order results
Result details
Results per page
Select all
Export citation of selected articles as:
15 pages, 2037 KB  
Article
Identification and Characterization of HIRIP3 as a Histone H2A Chaperone
by Maria Ignatyeva, Abdul Kareem Mohideen Patel, Abdulkhaleg Ibrahim, Raed S. Albiheyri, Ali T. Zari, Ahmed Bahieldin, Christian Bronner, Jamal S. M. Sabir and Ali Hamiche
Cells 2024, 13(3), 273; https://doi.org/10.3390/cells13030273 - 1 Feb 2024
Cited by 2 | Viewed by 2348
Abstract
HIRIP3 is a mammalian protein homologous to the yeast H2A.Z deposition chaperone Chz1. However, the structural basis underlying Chz’s binding preference for H2A.Z over H2A, as well as the mechanism through which Chz1 modulates histone deposition or replacement, remains enigmatic. In this study, [...] Read more.
HIRIP3 is a mammalian protein homologous to the yeast H2A.Z deposition chaperone Chz1. However, the structural basis underlying Chz’s binding preference for H2A.Z over H2A, as well as the mechanism through which Chz1 modulates histone deposition or replacement, remains enigmatic. In this study, we aimed to characterize the function of HIRIP3 and to identify its interacting partners in HeLa cells. Our findings reveal that HIRIP3 is specifically associated in vivo with H2A–H2B dimers and CK2 kinase. While bacterially expressed HIRIP3 exhibited a similar binding affinity towards H2A and H2A.Z, the associated CK2 kinase showed a notable preference for H2A phosphorylation at serine 1. The recombinant HIRIP3 physically interacted with the H2A αC helix through an extended CHZ domain and played a crucial role in depositing the canonical core histones onto naked DNA. Our results demonstrate that mammalian HIRIP3 acts as an H2A histone chaperone, assisting in its selective phosphorylation by Ck2 kinase at serine 1 and facilitating its deposition onto chromatin. Full article
(This article belongs to the Special Issue Epigenetics, Chromatin Structure and Transcription Regulation)
Show Figures

Figure 1

Back to TopTop