Thioredoxin-dependent disulfide bond reduction is required for protamine eviction from sperm chromatin

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

Cysteine oxidation in protamines leads to their oligomerization and contributes to sperm chromatin compaction. Here we identify the Drosophila thioredoxin Deadhead (DHD) as the factor responsible for the reduction of intermolecular disulfide bonds in protamines and their eviction fromsperm during fertilization. Protamine chaperone TAP/p32 dissociates DNA–protamine complexes in vitro only when protamine oligomers are first converted to monomers by DHD. dhd-null embryos cannot decondense sperm chromatin and terminate development after the first pronuclear division. Therefore, the thioredoxin DHD plays a critical role in early development to facilitate the switch from protamine-based sperm chromatin structures to the somatic nucleosomal chromatin.

Original languageEnglish (US)
Pages (from-to)2651-2656
Number of pages6
JournalGenes and Development
Volume30
Issue number24
DOIs
StatePublished - Dec 15 2016

Keywords

  • Disulfide bonds
  • Fertilization
  • Protamine eviction
  • Sperm chromatin remodeling
  • Thioredoxin system

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

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