Chromosome Condensation in Xenopus Mitotic Extracts Without Histone H1
- 24 December 1993
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 262 (5142), 2033-2035
- https://doi.org/10.1126/science.8266099
Abstract
The contribution of histone H1 to mitotic chromosome condensation was examined with the use of a cell-free extract from Xenopus eggs, which transforms condensed sperm nuclei into metaphase chromosomes. When H1 was removed from the extract, the resultant metaphase chromosomes were indistinguishable from those formed in complete extract. Nucleosomal spacing was the same for both. Thus, H1 is not required for the structural reorganization that leads to condensed metaphase chromosomes in this egg extract.Keywords
This publication has 34 references indexed in Scilit:
- Remodeling of Human Sperm Chromatin Mediated by Nucleoplasmin from Amphibian EggsDevelopment, Growth & Differentiation, 1993
- Characterization of the ooplasmic factor inducing decondensation of and protamine removal from toad sperm nuclei: Involvement of nucleoplasminDevelopmental Biology, 1991
- The topoisomerase II inhibitor VM-26 induces marked changes in histone H1 kinase activity, histones H1 and H3 phosphorylation, and chromosome condensation in G2 phase and mitotic BHK cells.The Journal of cell biology, 1990
- Universal control mechanism regulating onset of M-phaseNature, 1990
- Assembly and properties of chromatin containing histone H1Journal of Molecular Biology, 1989
- Human sperm nuclei can transform into condensed chromosomes in Xenopus egg extractsGamete Research, 1988
- Disassembly of the nucleus in mitotic extracts: Membrane vesicularization, lamin disassembly, and chromosome condensation are independent processesCell, 1987
- H1 histone variants in Xenopus laevisDevelopmental Biology, 1981
- Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin.The Journal of cell biology, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970