PMID: 2508749Nov 2, 1989Paper

Purification and properties of the DNA-binding protein HPB12 from Bacillus subtilis nucleoid

Biochimica Et Biophysica Acta
V SaltiL Hirschbein

Abstract

We report the purification to homogeneity of a 12 KDa protein (HPB12) present in the nucleoids of Bacillus subtilis. From the purification data the abundance of the protein was estimated to about 20,000 monomers per cell. The HPB12 protein is heat-stable and acid-soluble and binds preferentially to supercoiled and linearized double-stranded DNAs. The binding of the protein to the supercoiled DNA occurs very rapidly and appears to be cooperative. Moreover, the complexes are extremely stable and do not dissociate after 90 min. These properties are consistent with a role of the HPB12 protein in the structure of the B. subtilis chromosome.

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Citations

Jan 1, 1995·Micron : the International Research and Review Journal for Microscopy·M A Hayat, D A Mancarella
Feb 20, 1993·Biochimica Et Biophysica Acta·F Le HégaratL Hirschbein
Jan 1, 1994·Journal of Bacteriology·B Arnold-Schulz-GahmenF Le Hégarat
Oct 1, 1991·Journal of Bacteriology·B SetlowP Setlow

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