HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 279, Issue 22, 23525-23535, May 28, 2004

This Article Full Text Full Text (PDF) All Versions of this Article: 279/22/23525    most recent M400925200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lin, Q. Articles by Skoultchi, A. I. Search for Related Content PubMed PubMed Citation Articles by Lin, Q. Articles by Skoultchi, A. I. Social Bookmarking                      What's this?

Reductions in Linker Histone Levels Are Tolerated in Developing Spermatocytes but Cause Changes in Specific Gene Expression^*

Qingcong Lin, Amy Inselman¶||, Xing Han, Hui Xu, Weijia Zhang, Mary Ann Handel¶**, and Arthur I. Skoultchi

From the Department of Cell Biology, Albert Einstein College of Medicine, Bronx, New York 10461 and the ^¶Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996-0840

H1 linker histones are involved in packaging chromatin into 30-nm fibers and higher order structures. Most eukaryotic cells contain nearly one H1 molecule for each nucleosome core particle. Male germ cells in mammals contain large amounts of a germ cell-specific linker histone, HIST1HT, herein denoted H1t, which is particularly abundant in pachytene spermatocytes. Despite its abundance in male germ cells and significant divergence in primary sequence from other H1 subtypes, inactivation of the H1t gene in mice showed that it is not required for spermatogenesis. Analysis of germ cell chromatin from H1t null mice showed that other H1 subtypes, especially the testis-enriched HIST1H1A, herein denoted as the H1a subtype, were able to compensate for the absence of H1t to maintain a normal total H1 to nucleosome core ratio. To disrupt the compensation, we generated H1t and H1a double null mice by two sequential gene-targeting steps in embryonic stem cells. Elimination of both H1t and H1a led to a 25% decrease in the ratio of H1 to nucleosome cores in double null germ cells. Surprisingly, the reduction in H1 did not perturb spermatogenesis or produce detectable defects in meiotic processes. Microarray analysis of gene expression showed that the reduced linker histone levels did not affect global gene expression, but it did cause changes in expression of specific genes. Our results indicate that a partial reduction in linker histone-nucleosome core particle stoichiometry is tolerated in developing male germ cells.

Received for publication, January 28, 2004 , and in revised form, March 10, 2004.

^* This work was supported by National Institutes of Health Grants CA79057 (to A. I. S.) and HD33816 (to M. A. H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Current address: Harvard Partners Center for Genetics and Genomics, Massachusetts General Hospital, Harvard Medical School, 149, 13th St., 149-4325, Charlestown, MA 02129.

^|| Current address: Laboratory for Reproductive and Developmental Toxicology, NIEHS, National Institutes of Health, Research Triangle Park, NC 27709.

^** Current address: The Jackson Laboratory, 600 Main St., Bar Harbor, ME 04609.

To whom correspondence should be addressed: Dept. of Cell Biology, Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461. Tel.: 718-430-2169; Fax: 718-430-8574; E-mail: skoultch{at}aecom.yu.edu.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				J. S. Godde and K. Ura Cracking the Enigmatic Linker Histone Code J. Biochem., March 1, 2008; 143(3): 287 - 293. [Abstract] [Full Text] [PDF]

				P. B. Hebbar and T. K. Archer Altered Histone H1 Stoichiometry and an Absence of Nucleosome Positioning on Transfected DNA J. Biol. Chem., February 22, 2008; 283(8): 4595 - 4601. [Abstract] [Full Text] [PDF]

				I. Nagamori, K. Yomogida, M. Ikawa, M. Okabe, N. Yabuta, and H. Nojima The testes-specific bZip type transcription factor Tisp40 plays a role in ER stress responses and chromatin packaging during spermiogenesis. Genes Cells, October 1, 2006; 11(10): 1161 - 1171. [Abstract] [Full Text] [PDF]

				H K Kinyamu, J Chen, and T K Archer Linking the ubiquitin-proteasome pathway to chromatin remodeling/modification by nuclear receptors J. Mol. Endocrinol., April 1, 2005; 34(2): 281 - 297. [Abstract] [Full Text] [PDF]

				O. M. Alekseev, E. E. Widgren, R. T. Richardson, and M. G. O'Rand Association of NASP with HSP90 in Mouse Spermatogenic Cells: STIMULATION OF ATPase ACTIVITY AND TRANSPORT OF LINKER HISTONES INTO NUCLEI J. Biol. Chem., January 28, 2005; 280(4): 2904 - 2911. [Abstract] [Full Text] [PDF]

				X. Wang, Y. Peng, Y. Ma, and N. Jahroudi Histone H1-like protein participates in endothelial cell-specific activation of the von Willebrand factor promoter Blood, September 15, 2004; 104(6): 1725 - 1732. [Abstract] [Full Text] [PDF]