Lipocortin (Annexin) I heterotetramer binds to purine RNA and pyrimidine DNA.
Lipocortin I-like protein with a molecular weight of 94,000 Da as judged by Western analysis was found to bind to ssDNA rather than to dsDNA in a Ca(2+)-dependent manner. This protein was also bound to [(32)P]poly(rA) and [(32)P]poly(rG) as measured by EMSA. Poly(rG), poly(rA), poly(dC), and poly(dT) were competitive against binding of either [(32)P]poly(rA) or [(32)P]poly(rG), while poly(rC), poly(rU), and poly(dA) were less effective binding competitors. The binding of this protein to poly(rA) or poly(rG) was inhibited by immunoprecipitable anti-lipocortin I (calpactin II) and anti-S100 protein antibodies, but not by an anti-Ig antibody. Phospholipids such as phosphatidylserine and phosphatidylinositol enhanced the binding of lipocortin I to poly(rA). Taken together, our present observations suggest that the lipocortin I-S100 protein heterotetramer binds to either purine RNAs or pyrimidine ssDNAs in a Ca(2+)- and phospholipid-dependent manner.
Hirata
A
A
Department of Pharmaceutical Sciences, Wayne State University, Detroit, Michigan, 48202, USA.
Hirata
F
F
D000818:Animals; D017305:Annexin A1 / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D001665:Binding Sites; D002118:Calcium / Q000494:pharmacology; D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D004277:DNA, Single-Stranded / Q000737:chemistry / Q000378:metabolism; D008099:Liver / Q000378:metabolism; D046911:Macromolecular Substances; D008274:Magnesium / Q000494:pharmacology; D008297:Male; D010743:Phospholipids / Q000494:pharmacology; D011089:Polydeoxyribonucleotides / Q000378:metabolism; D011131:Polyribonucleotides / Q000378:metabolism; D012313:RNA / Q000737:chemistry / Q000378:metabolism*; D051381:Rats
D017305:Annexin A1; D004277:DNA, Single-Stranded; D046911:Macromolecular Substances; D010743:Phospholipids; D011089:Polydeoxyribonucleotides; D011131:Polyribonucleotides; D012313:RNA; D004247:DNA; D008274:Magnesium; D002118:Calcium