PURIFICATION AND CHARACTERIZATION OF THE HU-LIKE PROTEIN HPB9 FROM THE BACILLUS-SUBTILIS NUCLEOID

被引：0
作者：
LEHEGARAT, F
SALTIMONTESANTO, V
HAUCK, Y
HIRSCHBEIN, L
机构：
来源：
BIOCHIMICA ET BIOPHYSICA ACTA | 1993年 / 1172卷 / 1-2期
关键词：
DNA-BINDING; HISTONE-LIKE PROTEIN; SUPERCOILING; NUCLEOID; (BACILLUS-SUBTILIS);
D O I：
暂无
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The Bacillus subtilis HPB9 is the major heat-stable and acid-soluble protein associated with the nucleoid isolated at low ionic strength. The abundance of the protein in the cell is estimated to about 20 000 monomers per cell (Salti et al. (1985) J. Gen. Microbiol. 131, 581-590). The protein cross reacts specifically with the antiserum against the Bacillus globigii HBg. Moreover, HPB9 is able to introduce negative supercoiling in a relaxed covalently closed circular DNA, in the presence of topoisomerase I as demonstrated by one and two-dimensional electrophoresis. These results indicate that the nucleoid associated protein HPB9 is an HU-like protein and could be involved in the DNA compaction.
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页码：101 / 107
页数：7
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