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ATP-dependent DNA aggregation is a novel function of rat serum albumin.
- Source :
-
Archives of biochemistry and biophysics [Arch Biochem Biophys] 1991 Jun; Vol. 287 (2), pp. 367-71. - Publication Year :
- 1991
-
Abstract
- An ATP-dependent DNA aggregating activity was purified from rat liver by DEAE-cellulose, phosphocellulose, and novobiocin-Sepharose column chromatography. The protein aggregated superhelical, relaxed, single-, or double-stranded DNA in a divalent cation- and ATP-dependent reaction. The DNA aggregating activity was detected by retardation of a DNA-protein complex at the origin on a 1% agarose gel. The protein appeared to exist in solution as a monomer of molecular weight 66,000, and had no DNA polymerase, topoisomerase, recombinase, or ligase activity. The DNA aggregating activity was inhibited by 10 mM nalidixic acid or 1 mM novobiocin but not by 20 mM N-ethylmaleimide or camptothecin. Adenylyl(beta,gamma-methylene)-diphosphonate, adenylyl-imidodiphosphate, or adenosine-5'-O(3-thiotriphosphate) did not substitute for ATP whereas CTP, dTTP, or the ATP analog adenylyl(alpha,beta-methylene)-diphosphonate could replace ATP. The aggregated DNA was only partially dissociated by restriction endonuclease digestion but was completely dissociated by deproteinization with SDS, proteinase K, or chloroform/octanol extraction. On the basis of the molecular weight, thermostability, antigenic property, and amino acid sequence homology in the first 12 positions, we conclude that the rat liver protein is serum albumin and that the ATP-dependent DNA aggregation is a novel function of rat serum albumin.
- Subjects :
- Animals
Cations, Divalent
DNA drug effects
DNA, Circular drug effects
DNA, Circular metabolism
DNA, Single-Stranded drug effects
DNA, Single-Stranded metabolism
DNA, Superhelical drug effects
DNA, Superhelical metabolism
DNA, Viral drug effects
DNA, Viral metabolism
Drug Stability
Hot Temperature
Macromolecular Substances
Molecular Weight
Nalidixic Acid pharmacology
Novobiocin pharmacology
Rats
Rats, Inbred Strains
Sequence Homology, Nucleic Acid
Serum Albumin chemistry
Serum Albumin isolation & purification
Adenosine Triphosphate pharmacology
DNA metabolism
Liver chemistry
Serum Albumin pharmacology
Subjects
Details
- Language :
- English
- ISSN :
- 0003-9861
- Volume :
- 287
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Archives of biochemistry and biophysics
- Publication Type :
- Academic Journal
- Accession number :
- 1898009
- Full Text :
- https://doi.org/10.1016/0003-9861(91)90491-z