Poly(ADP-ribose) Metabolism Is Essential for Proper Nucleoprotein Exchange During Mouse Spermiogenesis

Sperm chromatin is organized in a protamine-based, highly condensed form, which protects the paternal chromosome complement in transit, facilitates fertilization, and supports correct gene expression in the early embryo. Very few histones remain selectively associated with genes and defined regulato...

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Bibliographic Details
Published in:Biology of reproduction 2011-02, Vol.84 (2), p.218-228
Main Authors: Meyer-Ficca, Mirella L, Ihara, Motomasa, Lonchar, Julia D, Meistrich, Marvin L, Austin, Caroline A, Min, Wookee, Wang, Zhao-Qi, Meyer, Ralph G
Format: Article
Language:English
Subjects:
Animals
Animals, Genetically Modified
Biological and medical sciences
Cell Nucleus - metabolism
Chromatin Assembly and Disassembly - physiology
DNA Breaks
DNA-Binding Proteins - metabolism
Fundamental and applied biological sciences. Psychology
Glycoside Hydrolases - metabolism
Histones - metabolism
Male
Mice
Nucleoproteins - metabolism
Poly (ADP-Ribose) Polymerase-1
Poly Adenosine Diphosphate Ribose - metabolism
Poly(ADP-ribose) Polymerases - metabolism
Spermatids - physiology
Spermatogenesis - physiology
Spermatozoa - metabolism
Vertebrates: reproduction
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Summary:Sperm chromatin is organized in a protamine-based, highly condensed form, which protects the paternal chromosome complement in transit, facilitates fertilization, and supports correct gene expression in the early embryo. Very few histones remain selectively associated with genes and defined regulatory sequences essential to embryonic development, while most of the genome becomes bound to protamine during spermiogenesis. Chromatin remodeling processes resulting in the dramatically different nuclear structure of sperm are poorly understood. This study shows that perturbation of poly(ADP-ribose) (PAR) metabolism, which is mediated by PAR polymerases and PAR glycohydrolase in response to naturally occurring endogenous DNA strand breaks during spermatogenesis, results in the abnormal retention of core histones and histone linker HIST1H1T (H1t) and H1-like linker protein HILS1 in mature sperm. Moreover, genetic or pharmacological alteration of PAR metabolism caused poor sperm chromatin quality and an abnormal nuclear structure in mice, thus reducing male fertility.
ISSN:0006-3363
1529-7268
DOI:10.1095/biolreprod.110.087361