Molecular characterization of a heat-modifiable protein from the outer membrane of Escherichia coli. |
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| Authors: | R A Reithmeier P D Bragg |
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| Institution: | Laboratory for Developmental Biology, Ethel Percy Andrus Gerontology Center, and Department of Biochemistry, School of Dentistry, University of Southern California, Los Angeles, California 90007 U.S.A. |
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| Abstract: | Discrete fractions of nonhistone chromosomal proteins (NHCP) were obtained from rabbit liver chromatin by their dissociation in 5 m urea with increasing concentrations of NaCl. Three fractions were obtained: M0, M1, and M3. We found that M0 can modify the conformation of DNA/histone complexes as depicted from their induced increase in the ellipticity of DNA/histone from 5100 to 6900 degree-cm2/dmol. This effect was found to be reversible, while M1 and M3 effects, if any, were not measurable. These results suggest that M0 primarily interacts with the chromatin subunit. |
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