Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M409415200 on September 27, 2004

J. Biol. Chem., Vol. 279, Issue 50, 51862-51868, December 10, 2004
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
279/50/51862    most recent
M409415200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Martins, R. P.
Right arrow Articles by Krawetz, S. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Martins, R. P.
Right arrow Articles by Krawetz, S. A.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Nuclear Matrix Interactions at the Human Protamine Domain

A WORKING MODEL OF POTENTIATION*

Rui Pires Martins{ddagger}, G. Charles Ostermeier§, and Stephen A. Krawetz{ddagger}§¶||

From the {ddagger}Center for Molecular Medicine and Genetics, the §Department of Obstetrics and Gynecology, and the Institute for Scientific Computing, Wayne State University, School of Medicine, Detroit, Michigan 48201

The compact eukaryotic genome must be selectively opened to grant trans-factor access to cis-regulatory elements to overcome the primary barrier to gene transcription. The mechanism that governs the selective opening of chromatin domains (i.e. potentiation) remains poorly understood. In the absence of a well defined locus control region, the nuclear matrix is considered the primary candidate regulating the opening of the multigenic PRM1 -> PRM2 -> TNP2 human protamine domain. To directly examine its role, four lines of transgenic mice with different configurations of flanking nuclear matrix attachment regions (MARs) encompassing the protamine domain were created. We show that upon removal of the MARs, the locus becomes subject to position effects. The 3' MAR alone may be sufficient to protect against silencing. In concert, the MARs bounding this domain likely synergize to regulate the expression of the various members of this gene cluster. Interestingly, the MARs may convey a selective reproductive advantage, such that constructs bearing both 5' and 3' MARs are passed to their offspring with greater frequency. Thus, the MARs bounding the PRM1 -> PRM2 -> TNP2 protamine domain have many and varied functions.


Received for publication, August 17, 2004 , and in revised form, September 20, 2004.

* This work was supported in part by National Institutes of Health Grant HD36512 (to S. A. K.) and by a predoctoral interdisciplinary biomedical sciences fellowship from the Wayne State University School of Medicine (to R. P. M.). The Transgenic Animal Model Core of the University of Michigan's Biomedical Research Core Facilities was funded in part by the Michigan Economic Development Council. 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.

|| To whom correspondence should be addressed: Dept. of Obstetrics and Gynecology, Molecular Medicine, and Genetics, Institute for Scientific Computing, Wayne State University School of Medicine, 275 E. Hancock, Detroit, MI 48201. Tel.: 313-577-6770; Fax: 313-577-8554; E-mail: steve{at}compbio.med.wayne.edu.


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


This article has been cited by other articles:


Home page
ReproductionHome page
D. C Wilkerson and K. D Sarge
RNA polymerase II interacts with the Hspa1b promoter in mouse epididymal spermatozoa
Reproduction, June 1, 2009; 137(6): 923 - 929.
[Abstract] [Full Text] [PDF]


Home page
Hum Mol GenetHome page
A. K. Linnemann, A. E. Platts, and S. A. Krawetz
Differential nuclear scaffold/matrix attachment marks expressed genes
Hum. Mol. Genet., February 15, 2009; 18(4): 645 - 654.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
R. P. Martins and S. A. Krawetz
Decondensing the protamine domain for transcription
PNAS, May 15, 2007; 104(20): 8340 - 8345.
[Abstract] [Full Text] [PDF]


Home page
Hum Reprod UpdateHome page
D. T. Carrell, B. R. Emery, and S. Hammoud
Altered protamine expression and diminished spermatogenesis: what is the link?
Hum. Reprod. Update, May 1, 2007; 13(3): 313 - 327.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
S. Hama, H. Akita, S. Iida, H. Mizuguchi, and H. Harashima
Quantitative and mechanism-based investigation of post-nuclear delivery events between adenovirus and lipoplex
Nucleic Acids Res., March 12, 2007; 35(5): 1533 - 1543.
[Abstract] [Full Text] [PDF]


Home page
Hum Reprod UpdateHome page
R. Oliva
Protamines and male infertility
Hum. Reprod. Update, July 1, 2006; 12(4): 417 - 435.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2004 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement