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Previously uncharacterized histone acetyltransferases implicated in mammalian spermatogenesis.

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Previously uncharacterized histone acetyltransferases implicated in mammalian spermatogenesis.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Barndt, Robert J. Parvinen, Martti Lahn, Bruce T. Allis, C. David Page, David C. Tang, Zhao Lan Zhou, Jianxin
Description	Author Affiliation: Lahn BT ( Howard Hughes Medical Institute, Department of Human Genetics, University of Chicago, Chicago, IL 60637, USA. blahn@genetics.uchicago.edu);
Abstract	During spermiogenesis (the maturation of spermatids into spermatozoa) in many vertebrate species, protamines replace histones to become the primary DNA-packaging protein. It has long been thought that this process is facilitated by the hyperacetylation of histone H4. However, the responsible histone acetyltransferase enzymes are yet to be identified. CDY is a human Y-chromosomal gene family expressed exclusively in the testis and implicated in male infertility. Its mouse homolog Cdyl, which is autosomal, is expressed abundantly in the testis. Proteins encoded by CDY and its homologs bear the 'chromodomain,' a motif implicated in chromatin binding. Here, we show that (i) human CDY and mouse CDYL proteins exhibit histone acetyltransferase activity in vitro, with a strong preference for histone H4; (ii) expression of human CDY and mouse Cdyl genes during spermatogenesis correlates with the occurrence of H4 hyperacetylation; and (iii) CDY and CDYL proteins are localized to the nuclei of maturing spermatids where H4 hyperacetylation takes place. Taken together, these data link human CDY and mouse CDYL to the histone-to-protamine transition in mammalian spermiogenesis. This link offers a plausible mechanism to account for spermatogenic failure in patients bearing deletions of the CDY genes.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	13
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Acetyltransferases Physiology Nuclear Proteins Saccharomyces Cerevisiae Proteins Spermatogenesis Acetylation Metabolism Amino Acid Sequence Animals DNA Primers Histone Acetyltransferases Histones Immunohistochemistry Mice Molecular Sequence Data Proteins Genetics Reverse Transcriptase Polymerase Chain Reaction Sequence Homology, Amino Acid Spermatids Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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