title: Proteins of Caulobacter crescentus strongly binding to DNA. Spectroscopic analysis of major histone-like proteins.
abstract: The protein composition of deoxyribonucleoprotein (DNP) from Caulobacter crescentus, protected from exogenous nucleases, was analysed. This fraction was obtained by purification of cell lysate on Sephacryl S-400. It contained the following proteins: 13.4 kDa (HCc), 15.2 kDa, 17.5 kDa, 28 kDa and 40 kDa. The strength of protein 15.2 kDa binding to ds-DNA was the same as that of the eukaryotic histones H2A and H2B. Proteins 13.4 kDa (HCc) and 17.5 kDa purified to homogeneity have a UV spectrum identical to protein HU of Escherichia coli which lacks tryptophane and tyrosine. This confirms the classification of protein HCc to the class of HU-like proteins.
authors.affiliation: Department of Bacterial Physiology, University of Warsaw, Poland.
authors.forename: B
authors.initials: B
authors.lastname: Paterczyk
authors.forename: J
authors.initials: J
authors.lastname: Fornal
mesh_terms: D001426:Bacterial Proteins / Q000032:analysis / Q000302:isolation & purification*; D016935:Caulobacter crescentus / Q000737:chemistry*; D002852:Chromatography, Ion Exchange; D004268:DNA-Binding Proteins / Q000032:analysis / Q000302:isolation & purification*; D003852:Deoxyribonucleoproteins / Q000302:isolation & purification; D004586:Electrophoresis; D013056:Spectrophotometry, Ultraviolet
chemical_list: D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D003852:Deoxyribonucleoproteins