Aspects of Interaction of Putative Anchorosomal Protein p68 with the Nuclear Envelope during the Cell Cycle

Aspects of Interaction of Putative Anchorosomal Protein p68 with the Nuclear Envelope during the... In the interphase nucleus, the chromatin associated with the nuclear envelope is represented by a layer of anchorosomes, granules with a diameter of 20–25 nm. Biochemically, the fraction of chromatin directly associated with the nuclear envelope is characterized by resistance against decondensing influences, a low level of DNA methylation, and presence of specific acid-soluble proteins. However, the mechanisms lying at the base of chromatin-nuclear envelope interaction have been insufficiently studied. Specifically, it is unknown whether anchorosomes are constant structures or subject to reversible disassembly, when the contacts between chromatin and nuclear envelope are destroyed. We obtained immune serum recognizing a 68 kDa protein from the nuclear envelopes fraction and studied the localization of this protein in interphase and mitotic cells. We show that this protein, present in the NE/anchorosomal fraction, does not remain bound with chromosomes during mitosis. It dissociates from chromosomes at the beginning of the prophase and then can be identified again at the periphery of the newly forming nuclei in the telophase. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Developmental Biology Springer Journals

Aspects of Interaction of Putative Anchorosomal Protein p68 with the Nuclear Envelope during the Cell Cycle

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Publisher
Springer Journals
Copyright
Copyright © 2000 by MAIK “Nauka/Interperiodica”
Subject
Life Sciences; Animal Anatomy / Morphology / Histology
ISSN
1062-3604
eISSN
1608-3326
D.O.I.
10.1023/A:1026635014739
Publisher site
See Article on Publisher Site

Abstract

In the interphase nucleus, the chromatin associated with the nuclear envelope is represented by a layer of anchorosomes, granules with a diameter of 20–25 nm. Biochemically, the fraction of chromatin directly associated with the nuclear envelope is characterized by resistance against decondensing influences, a low level of DNA methylation, and presence of specific acid-soluble proteins. However, the mechanisms lying at the base of chromatin-nuclear envelope interaction have been insufficiently studied. Specifically, it is unknown whether anchorosomes are constant structures or subject to reversible disassembly, when the contacts between chromatin and nuclear envelope are destroyed. We obtained immune serum recognizing a 68 kDa protein from the nuclear envelopes fraction and studied the localization of this protein in interphase and mitotic cells. We show that this protein, present in the NE/anchorosomal fraction, does not remain bound with chromosomes during mitosis. It dissociates from chromosomes at the beginning of the prophase and then can be identified again at the periphery of the newly forming nuclei in the telophase.

Journal

Russian Journal of Developmental BiologySpringer Journals

Published: Oct 8, 2004

References

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