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J. Biochem, 1988, Vol. 104, No. 1 127-130
© 1988 Japanese Biochemical Society

research-article

Isolation of a DNA-Binding Protein from Deinococcus radiodurans Having an Affinity for a Z-Form Polynucleotide1

Shigeru Kitayama2, Osamu Matsumura and Susumu Masuda

Radiobiology Laboratory, The Institute of Physical and Chemical Research Wako, Saitama 351-01

2 To whom correspondence should be addressed

A protein which preferentially binds Z-form duplex DNA has been purified from the cells of Deinococcus radiodurans. The molecular weight of the protein was estimated to be approximately 68,000 by gel filtration and SDS-polyacrylamide gel electrophoresis. Amino acid analysis of the protein indicates that it is not so basic since it contains a lower mole percent of lysine and higher mole percent of aspartic acid than those in histone-like DNA binding protein II (HU) of Escherichia coil. The first fifteen amino acid residues from the N-terminus have been also determined.

1 This study was partly supported by grants from this Institute and Kaken Seiyaku Co., Ltd.


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