SIRT1 retention in elongating spermatids interferes with histone displacement by counteracting MOF-dependent H4K16 acetylation.

ABSTRACT:

Introduction

The histone H4 hyperacetylation (i.e., acetylation of H4 at lysines -K5, -K8, -K12, and -K16, here reported as H4tetraAc) occurs in elongating spermatids (eSPTs) during spermiogenesis. Although it is critically involved in histone displacement, the mechanistic involvement of histone -acetyltransferases (HATs) and -deacetylases (HDACs) in the pathway underlying H4 hyperacetylation is poorly defined. Here, we investigate the involvement of SIRT1 deacetylase, and its functional interaction with the histone acetyltransferase MOF, in regulating H4 hyperacetylation underlying histone-to-protamine exchange.

Methods

Exploiting the cannabinoid receptor 1 (Cb1) null mice (Cb1^-/-) as a model of impaired histone displacement, we assessed in eSPTs the expre

SUBMITTER: Porreca V 

PROVIDER: S-EPMC12426168 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature