Purification and the histones of Dictyostelium discoideum chromatin

Creators: Bakke, Antony C.; Bonner, James

Abstract

Dictyostelium chromatin has been purified from nuclei in high yield by differential centrifugation and nuclease cleaving. Its chemical composition has been assayed, and its histones have been analyzed by gel electrophoresis, peptide fingerprints, amino acid composition, and ion-exchange chromatography. The mass ratios of DNA/RNA/histone nonhistone are 1.0:0.18:0.98: 1.02. There are four histones including one unusual histone, H7, which is the most abundant histone in the slime mold. The H4-like protein is the most conserved protein, while the other histones show both similarities and differences with mammalian histones.

Additional Information

© 1979 American Chemical Society. Received November 18, 1977; revised manuscript received July 13, 1979. Supported in part by U.S. Public Health Service Grant GM 13762 and U.S. Public Health Service Training Grants GM 00086 and GM 07437-02. This is publication no. 125 from the Department of Cellular and Developmental Immunology and no. 1849 from the Research Institute of Scripps Clinic. We thank Dr. J. R. Wu for helpful suggestions and critical evaluation of the manuscript, R. F. Murphy for assistance with the computer evaluation of the data, and B. Eurich for reviewing the manuscript. Dr. J. H. Elder was very helpful in giving instructions for the peptide mapping technique, and P. Segrist ran the amino acid analyzer. We also thank Dr. R. B. Wallace, T. D. Sargent, and Dr. A. R. Chilina for many stimulating discussions. Dr. R. A. Lerner kindly provided time and encouragement to complete these studies.

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Resource type: Journal Article
Publisher: American Chemical Society
Published in: Biochemistry, 18(21), 4556-4562, ISSN: 0006-2960.