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5 July 2021 RNF8 is not required for histone-to-protamine exchange in spermiogenesis
Hironori Abe, Rajyalakshmi Meduri, Ziwei Li, Paul R. Andreassen, Satoshi H. Namekawa
Author Affiliations +
Abstract

While an E3 ubiquitin ligase, RNF8, was initially reported to be required for histone-to-protamine exchange in spermiogenesis, we subsequently demonstrated that RNF8 is not involved in this process. Nevertheless, reflecting a lingering misunderstanding in the field, a growing number of studies have continued to postulate a requirement for RNF8 in the histone-to-protamine exchange. For example, a recent study claimed that a mouse PIWI protein, MIWI, controls RNF8-mediated histone-to-protamine exchange. Here, confirming our earlier conclusions, we show that RNF8 is required neither for the establishment of histone H4K16 acetylation, which is an initial step in histone removal during spermiogenesis, nor for the incorporation of two protamine proteins, PRM1 and PRM2. Thus, whereas RNF8 mediates ubiquitination of H2A on the sex chromosomes in meiosis, during the prior stage of spermatogenesis, our genetic evidence underscores that RNF8 is not involved in histone-to-protamine exchange.

Summary sentence

Given controversy in the field, we rigorously re-examined the function of RNF8 and conclude that RNF8 is required for ubiquitination of the sex chromosomes during meiosis but not for histone-to-protamine exchange during spermiogenesis.

© The Author(s) 2021. Published by Oxford University Press on behalf of Society for the Study of Reproduction. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com
Hironori Abe, Rajyalakshmi Meduri, Ziwei Li, Paul R. Andreassen, and Satoshi H. Namekawa "RNF8 is not required for histone-to-protamine exchange in spermiogenesis," Biology of Reproduction 105(5), 1154-1159, (5 July 2021). https://doi.org/10.1093/biolre/ioab132
Received: 19 February 2021; Accepted: 2 July 2021; Published: 5 July 2021
KEYWORDS
histone-to-protamine exchange
MIWI
RNF8
sperm
spermiogenesis
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