A polarized photobleaching study of chromatin reorientation in intact nuclei
dc.contributor.author | Selvin, Paul R. | en_US |
dc.contributor.author | Scalettar, Bethe A. | en_US |
dc.contributor.author | Langmore, John P. | en_US |
dc.contributor.author | Axelrod, Daniel | en_US |
dc.contributor.author | Klein, Melvin P. | en_US |
dc.contributor.author | Hearst, John E. | en_US |
dc.date.accessioned | 2006-04-10T13:38:11Z | |
dc.date.available | 2006-04-10T13:38:11Z | |
dc.date.issued | 1990-08-20 | en_US |
dc.identifier.citation | Selvin, Paul R., Scalettar, Bethe A., Langmore, John P., Axelrod, Daniel, Klein, Melvin P., Hearst, John E. (1990/08/20)."A polarized photobleaching study of chromatin reorientation in intact nuclei." Journal of Molecular Biology 214(4): 911-922. <http://hdl.handle.net/2027.42/28423> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WK7-4DMP2X4-W/2/775f0367619be3e93f209679da5d2d03 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/28423 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2388274&dopt=citation | en_US |
dc.description.abstract | Polarized fluorescence recovery after photobleaching (pFRAP) was used to monitor the effects that condensation, i.e. compaction and aggregation, have on the ([mu]s and ms) internal dynamics of chromatin in intact nuclei. When divalent cations were present with physiological ([approximate] 90 m) monovalent salt the chromatin was found to exist in a compact and aggregated state which was characterized by rotational immobilization over timescales that range from 10 microseconds to 40 milliseconds. This immobilization is attributed to suppression of internal dynamics by intermolecular interactions. When the divalent cations were removed, the compact fibers no longer aggregated and were free to reorient with a characteristic decay time of about 1.2 milliseconds. It is shown that this millisecond relaxation could represent rigid rotation of topologically independent structural domains. Dilution of the monovalent salt induced a gradual change in the structural state of the chromatin that was manifest as a dramatic increase in internal flexibility. At the lowest salt concentration studied (11 m-monovalent salt) the chromatin reorients in fewer than ten microseconds. These changes in flexibility are continuous with salt concentration, indicating that there are no well-defined endpoints to structural transitions and that the microsecond-millisecond internal dynamics of chromatin are a sensitive measure of structure. Measurements made on nuclei from cells that are either transcriptionally quiescent or active indicate that the dynamics mirrors biological activity. | en_US |
dc.format.extent | 1544570 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | A polarized photobleaching study of chromatin reorientation in intact nuclei | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biology University of Michigan, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Physics University of Michigan, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.contributor.affiliationother | Department of Physics University of California, Berkeley, CA 94720, U.S.A.; Chemical Biodynamics Division Lawrence Berkeley Laboratory, Berkeley, CA 94720, U.S.A. | en_US |
dc.contributor.affiliationother | Chemical Biodynamics Division Lawrence Berkeley Laboratory, Berkeley, CA 94720, U.S.A. | en_US |
dc.contributor.affiliationother | Chemical Biodynamics Division Lawrence Berkeley Laboratory, Berkeley, CA 94720, U.S.A. | en_US |
dc.contributor.affiliationother | Department of Chemistry University of California, Berkeley, CA 94720, U.S.A.; Chemical Biodynamics Division Lawrence Berkeley Laboratory, Berkeley, CA 94720, U.S.A. | en_US |
dc.identifier.pmid | 2388274 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/28423/1/0000206.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0022-2836(90)90345-M | en_US |
dc.identifier.source | Journal of Molecular Biology | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.