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Your search keyword '"Jansen, L. E. T."' showing total 5 results
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5 results on '"Jansen, L. E. T."'

1. Esperanto for histones: CENP-A, not CenH3, is the centromeric histone H3 variant

Author

Earnshaw, W. C., Allshire, R. C., Black, B. E., Bloom, K., Brinkley, B. R., Brown, W., Cheeseman, I. M., Choo, K. H. A., Copenhaver, G. P., DeLuca, J. G., Desai, A., Diekmann, S., Erhardt, S., Fitzgerald-Hayes, M., Foltz, D., Fukagawa, T., Gassmann, R., Gerlich, D. W., Glover, D. M., Gorbsky, G. J., Harrison, S. C., Heun, P., Hirota, T., Jansen, L. E. T., Karpen, G., Kops, G. J. P. L., Lampson, M. A., Lens, S. M., Losada, A., Luger, K., Maiato, H., Maddox, P. S., Margolis, R. L., Masumoto, H., McAinsh, A. D., Mellone, B. G., Meraldi, P., Musacchio, A., Oegema, K., O’Neill, R. J., Salmon, E. D., Scott, K. C., Straight, A. F., Stukenberg, P. T., Sullivan, B. A., Sullivan, K. F., Sunkel, C. E., Swedlow, J. R., Walczak, C. E., Warburton, P. E., Westermann, S., Willard, H. F., Wordeman, L., Yanagida, M., Yen, T. J., Yoda, K., and Cleveland, D. W.

Published
2013
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2. Chromosomes. CENP-C reshapes and stabilizes CENP-A nucleosomes at the centromere

Author

Falk, S. J., Guo, L. Y., Sekulic, N., Smoak, E. M., Mani, T., Logsdon, G. A., Gupta, K., Jansen, L. E. T., Van Duyne, G. D., Vinogradov, S. A., Lampson, M. A., and Black, B. E.

Subjects
Chromosomal Proteins, Non-Histone, Gene Knockdown Techniques, education, Centromere, Fluorescence Resonance Energy Transfer, Humans, macromolecular substances, DNA, Autoantigens, Protein Structure, Secondary, Epigenesis, Genetic, Nucleosomes
Abstract

Inheritance of each chromosome depends upon its centromere. A histone H3 variant, centromere protein A (CENP-A), is essential for epigenetically marking centromere location. We find that CENP-A is quantitatively retained at the centromere upon which it is initially assembled. CENP-C binds to CENP-A nucleosomes and is a prime candidate to stabilize centromeric chromatin. Using purified components, we find that CENP-C reshapes the octameric histone core of CENP-A nucleosomes, rigidifies both surface and internal nucleosome structure, and modulates terminal DNA to match the loose wrap that is found on native CENP-A nucleosomes at functional human centromeres. Thus, CENP-C affects nucleosome shape and dynamics in a manner analogous to allosteric regulation of enzymes. CENP-C depletion leads to rapid removal of CENP-A from centromeres, indicating their collaboration in maintaining centromere identity. NIH grants: (GM082989, CA186430, GM008275, GM008216, GM007229); American Heart Association predoctoral fellowship; American Cancer Society postdoctoral fellowship; NSF grant: (agreement DMR-0944772).

Published
2015

3. Genetics. Sowing the seeds of centromeres

Author

Jansen, L. E. T.

Subjects
Histones, Centromere, Animals, Drosophila
Abstract

The centromere is a chromatin-based platform that accumulates microtubule-binding proteins that drive chromosome segregation during cell division. Despite their size (on the order of megabases of DNA in mammals) and conserved role, centromeres have the remarkable capacity to leave their usual comfort zone and to reform at a new chromosomal site (1). Although found rarely, these so-called neocentromeres are by most measures bona fide and segregate chromosomes with high fidelity. What accounts for this nomadic behavior?

Published
2012

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