Semihistone protein A24 replaces H2A as an integral component of the nucleosome histone core. Academic Article

abstract

• The semihistone protein, A24, was shown to be a stable minor component of purified salt-washed nucleosome core particles. A24 was also shown to become integrated into nucleohistone during reconstitution in a manner characteristic of the core histones. Purified A24 in solution was shown to exhibit the same specificity of interaction with histone H2B as is exhibited by histone H2A. We conclude that A24 in chromatin replaces H2A as a stable integral component of certain nucleosome histone cores.

authors

• Kunkel, Gary

published proceedings

• Proc Natl Acad Sci U S A

author list (cited authors)

• Martinson, H. G., True, R., Burch, J. B., & Kunkel, G

citation count

• 43

complete list of authors

• Martinson, HG||True, R||Burch, JB||Kunkel, G

publication date

• March 1979

publisher

• Proceedings of the National Academy of Sciences  Publisher

published in

• Proceedings of the National Academy of Sciences of the United States of America  Journal

keywords

• Animals
• Cattle
• Cell Nucleus
• Chromatin
• Deoxyribonucleoproteins
• Histones
• Macromolecular Substances
• Molecular Weight
• Nucleoproteins
• Sodium Chloride
• Thymus Gland

PubMed Central ID

• 286291

Digital Object Identifier (DOI)

• 10.1073/pnas.76.3.1030

start page

• 1030

end page

• 1034

volume

• 76

issue

• 3

URL

• http://dx.doi.org/10.1073/pnas.76.3.1030