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Published online 27 December 2000. doi:10.1083/jcb.151.7.1591
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© The Rockefeller University Press, 0021-9525/2000/12/1591/ $5.00
The Journal of Cell Biology, Volume 151, Number 7, December 25, 2000 1591-1598

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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

Correspondence to: Andrei O. Zalensky, Department of Biological Chemistry, School of Medicine, University of California at Davis, Tupper Hall, Davis, CA 95616. Tel:(530) 752-3314 Fax:(530) 752-3516 E-mail: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


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