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. 2000 Dec 25;151(7):1591–1598. doi: 10.1083/jcb.151.7.1591

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© 2000 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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Sperm-specific variant of human histone H2B is a component of hSTBP_TR. (a) Antibodies against H2B, but not against other histone fractions suppress formation of hSTBP-[TTAGGG]₁₂ complexes. Telomere binding activity was determined in gel-shift assay in the presence of the indicated antibodies. (b) Formation of the hSTBP-[TTAGGG]₁₂ complex was restored after preincubation of anti–H2B serum with the purified HeLa H2B. (c) Western analysis of acid-soluble and Triton X-100–extracted proteins of human sperm. (d–g) Partial purification of hSTBP_TR shows that spH2B histone coelutes with telomere-binding activity. Gel filtration: eluted fractions were assayed for telomere-binding activity (d), and Western blotting using anti–H2B antibodies (e). Ion-exchange chromatography: fractions were eluted by linear gradient of KCl, assayed for binding to [TTAGGG]₁₂ probe (f) and in Western blotting (g).

Sperm-specific variant of human histone H2B is a component of hSTBP_TR. (a) Antibodies against H2B, but not against other histone fractions suppress formation of hSTBP-[TTAGGG]₁₂ complexes. Telomere binding activity was determined in gel-shift assay in the presence of the indicated antibodies. (b) Formation of the hSTBP-[TTAGGG]₁₂ complex was restored after preincubation of anti–H2B serum with the purified HeLa H2B. (c) Western analysis of acid-soluble and Triton X-100–extracted proteins of human sperm. (d–g) Partial purification of hSTBP_TR shows that spH2B histone coelutes with telomere-binding activity. Gel filtration: eluted fractions were assayed for telomere-binding activity (d), and Western blotting using anti–H2B antibodies (e). Ion-exchange chromatography: fractions were eluted by linear gradient of KCl, assayed for binding to [TTAGGG]₁₂ probe (f) and in Western blotting (g).