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J Bacteriol. 1974 December; 120(3): 1443-1450
Copyright © 1974 American Society for Microbiology. All Rights Reserved.
a Department of Microbiology, Scripps Clinic and Research Foundation, La Jolla, California 92037
ABSTRACT
The isolation of deoxyribonucleic acid (DNA)-binding proteins from various stages of growth and sporulation of Bacillus subtilis is described. After adsorption and elution from phosphocellulose, the proteins were fractionated according to their ability to adsorb to denatured calf thymus DNA-cellulose or native B. subtilis DNA-cellulose. The proteins were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and purification was monitored by a nitrocellulose filter binding assay. Approximately 1% of the proteins in the crude extract adsorbed to denatured calf thymus DNA-cellulose and 0.1% adsorbed to native B. subtilis DNA-cellulose. Each class of proteins varied qualitatively and quantitatively as sporulation proceeded. Several proteins from the exponential phase of growth that bound to denatured DNA were lost by T0, whereas at T5 new polypeptides appeared. Fewer changes in the profile of proteins with affinity for native DNA were observed between exponential phase and T0; however, the dominant species in these eluates were clearly different.
1 Visiting scientist from the University of Paris, Centre d'Orsay, Laboratorie de Biologie Experimentale, France.
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