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Nucleic Acids Research, 1990, Vol. 18, No. 23 7015-7024
© 1990

Articles

Ultrastructure of transcriptionally competent chromatin

Lonzell Locklear, Jr, Andrew J. Ridsdale1, David P. Bazett-Jones* and James R. Davie1

Department of Medical Biochemistry, The University of Calgary 3330 Hospital Drive NW, Calgary, Alberta T2N 4N1, Canada 1Department of Biochemistry and Molecular Biology, University of Manitoba 770 Bannatyne Avenue, Winnipeg, Manitoba R3E 0W3, Canada

* To whom correspondence should be addressed

Received July 26, 1990. Revised November 2, 1990. Accepted November 2, 1990.

We have examined a salt-soluble, transcriptionally competent gene-enriched fraction of chicken erythrocyte chromatin and compared it to bulk chromatin using the unique mlcroanalytical capabilities of Electron Spectroscopic Imaging (ESI). The salt soluble fraction is enriched 48 fold in (ß-globln gene sequences and is also enriched in histones that are post-synthetically modified, including acetylation and ubiquitination. Differences between the two fractions are also apparent In the distribution of the two major forms of nucleoprotein structures, Including (1) particles which present a circular profile and possess protein and DNA content nearly identical to that of the canonical nucleosome and account for 89% of particles In the bulk fraction but account for only 66% of the particles in the competent fraction, and (2) u-shaped particles which possess about 20% less protein mass than particles of circular profile and are about 10x more prevalent In the transcriptionally competent fraction than in the bulk. Additionally, elongated particles with protein and DNA content similar to the u-shaped objects are also seen in the competent fraction.


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