Human milk lactoferrin binds two DNA molecules with different affinities.
Evidence is presented that lactoferrin (LF), an Fe3+-binding glycoprotein, possesses two DNA-binding sites with different affinities for specific oligonucleotides (ODNs) (Kdl = 8 nM; Kd2 approximately 0.1 mM). The high affinity site became labeled after incubation with affinity probes for DNA-binding sites; like the antibacterial and polyanion-binding sites, this site was shown to be located in the N-terminal domain of LF. Interaction of heparin with the polyanion-binding site inhibits the binding of ODNs to both sites. These data suggest that the DNA-binding sites of LF coincide or overlap with the known polyanion and antimicrobial domains of the protein.
Kanyshkova
T G
TG
Novosibirsk Institute of Bioorganic Chemistry, Siberian Division of Russian Academy of Sciences.
Semenov
D V
DV
Buneva
V N
VN
Nevinsky
G A
GA
D000890:Anti-Infective Agents / Q000378:metabolism; D001665:Binding Sites; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism; D005260:Female; D006801:Humans; D007781:Lactoferrin / Q000378:metabolism*; D008895:Milk, Human / Q000378:metabolism*; D011485:Protein Binding
D000890:Anti-Infective Agents; D004268:DNA-Binding Proteins; D004247:DNA; D007781:Lactoferrin