JCB logo
MBL International Tel: 800.200.5459 CLICK HERE
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online 25 December 2000. doi:10.1083/jcb.151.7.1591
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 399K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gineitis, A. A.
Right arrow Articles by Zalensky, A. O.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gineitis, A. A.
Right arrow Articles by Zalensky, A. O.
Related Collections
Right arrowRelated Article
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

© The Rockefeller University Press, 0021-9525/2000//1591 $5.00
The Journal of Cell Biology, Volume 151, Number 7, , 2000 1591-1598

Report

Human Sperm Telomere–Binding Complex Involves Histone H2b and Secures Telomere Membrane Attachment



Arunas A. Gineitisa,b, Irina A. Zalenskayaa, Peter M. Yaua, E. Morton Bradburya,c, and Andrei O. Zalenskya

a Department of Biological Chemistry, School of Medicine, University of California at Davis, Davis, California 95616
b Institute of Biochemistry, Lithuanian Academy of Sciences, Vilnius, Lithuania 2001
c Life Sciences Division, Los Alamos National Laboratory, Los Alamos, New Mexico 87545
Department of Biological Chemistry, School of Medicine, University of California at Davis, Tupper Hall, Davis, CA 95616.(530) 752-3516(530) 752-3314

aozalensky{at}ucdavis.edu

Telomeres are unique chromatin domains located at the ends of eukaryotic chromosomes. Telomere functions in somatic cells involve complexes between telomere proteins and TTAGGG DNA repeats. During the differentiation of germ-line cells, telomeres undergo significant reorganization most likely required for additional specific functions in meiosis and fertilization. A telomere-binding protein complex from human sperm (hSTBP) has been isolated by detergent treatment and was partially purified. hSTBP specifically binds double-stranded telomeric DNA and does not contain known somatic telomere proteins TRF1, TRF2, and Ku. Surprisingly, the essential component of this complex has been identified as a specific variant of histone H2B. Indirect immunofluorescence shows punctate localization of H2B in sperm nuclei, which in part coincides with telomeric DNA localization established by fluorescent in situ hybridization. Anti–H2B antibodies block interactions of hSTBP with telomere DNA, and spH2B forms specific complex with this DNA in vitro, indicating that this protein plays a role in telomere DNA recognition. We propose that hSTBP participates in the membrane attachment of telomeres that may be important for ordered chromosome withdrawal after fertilization.

Key Words: sperm • telomere • histone H2B • nuclear membrane

© 2000 The Rockefeller University Press

Arunas A. Gineitis and Irina A. Zalenskaya contributed equally to the paper and should be considered co–first authors.

Abbreviations used in this paper: dsTEL DNA, double-stranded telomere DNA; FISH, fluorescent in situ hybridization; hSTBP, human sperm telomere binding complex; spH2B, sperm-specific variant of histone H2B.


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 Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?

Related Article


J. Cell Biol. 2000 151: 0-2. [Full Text] [PDF]





  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents