Isolation and characterization of DNA-binding proteins from the cyanobacterium Synechococcus sp. PCC 7002 (Agmenellum quadruplicatum) and from spinach chloroplasts.
Basic, low-molecular-weight DNA-binding proteins were isolated from the unicellular cyanobacterium Synechococcus sp. PCC 7002 (Agmenellum quadruplicatum) and from the chloroplasts of spinach (Spinacia oleacera). In Synechococcus, two major proteins which bind to double-strand DNA (10 and 16 kDa, respectively) were purified. The 10 kDa protein, named HAq, resembles strongly, in amino-acid composition, eubacterial HU-type proteins. The 16 kDa protein is slightly basic. Its characteristics are compared to those of E. coli protein H1 and 17K. In spinach chloroplasts, a major protein HC (10 kDa), which also binds to ds-DNA, was purified. As observed for known archaebacterial and mitochondrial DNA-binding proteins, its amino-acid composition differs significantly from those of eubacterial HU. The comparison of the amino-terminal sequence (27 residues) with other chloroplast peptidic sequences is discussed.
Crevel
G
G
ER 308 CNRS, Laboratoire de Bioénergétique Cellulaire, Gif sur Yvette, France.
Laine
B
B
Sautière
P
P
Galleron
C
C
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002736:Chloroplasts / Q000032:analysis*; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D000458:Cyanobacteria / Q000032:analysis* / Q000235:genetics; D004247:DNA / Q000032:analysis; D004268:DNA-Binding Proteins / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000032:analysis; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010802:Phylogeny; D059828:Plant Cells; D010944:Plants / Q000032:analysis
D000596:Amino Acids; D004268:DNA-Binding Proteins; D004247:DNA