Isolation and characterization of small heat-stable acid-soluble DNA-binding proteins from Bacillus subtilis nucleoids.
Small heat-stable, acid-soluble proteins (HASP) have been isolated from Bacillus subtilis nucleoids obtained from cell lysates of low ionic strength and lysozyme concentration. They were identified by their ability to bind homologous and heterologous native and denatured DNA. Four major species, of 8.5, 12, 23 and 26 kDal, were found. Their affinity for DNA was moderate as measured by the sensitivity to ionic strength of the DNA-protein complex (0.1-0.4 M-NaCl). Partial digestion by micrococcal nuclease of the 'low ionic strength nucleoids' released a DNA fragment of 80-120 bp. The data reported here indicate that small basic proteins, together with other components such as RNA, cations and polyamines, may be involved in the compaction of the prokaryotic genome.
D001345:Autoradiography; D001412:Bacillus subtilis / Q000032:analysis*; D002846:Chromatography, Affinity; D004269:DNA, Bacterial / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000302:isolation & purification* / Q000378:metabolism; D004587:Electrophoresis, Agar Gel; D004591:Electrophoresis, Polyacrylamide Gel; D009994:Osmolar Concentration
D004269:DNA, Bacterial; D004268:DNA-Binding Proteins