Purification and characterization of the HU-like protein HPB9 from the Bacillus subtilis nucleoid.
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.
Le Hégarat
F
F
Institut de Génétique et Microbiologie, Université Paris-Sud, Orsay, France.
Salti-Montesanto
V
V
Hauck
Y
Y
Hirschbein
L
L
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000378:metabolism*; D001426:Bacterial Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002467:Cell Nucleus / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D003429:Cross Reactions; D004268:DNA-Binding Proteins / Q000302:isolation & purification*; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D007106:Immune Sera; D008969:Molecular Sequence Data; D008970:Molecular Weight
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D007106:Immune Sera; C040330:histone-like protein HU, bacteria