ABSTRACT
The central dogma of molecular genetics states that genetic information flows from DNA to RNA to protein. The nonhistone proteins that can interact with DNA sequences can be subdivided into two broad functional classes. Those that can interact with DNA in a catalytic fashion and those that interact stoichiometrically and hence act as structural proteins. The study of DNA-binding proteins rests with proteins which act on DNA during replication, recombination, and gene expresson. Unlike helix destabilizing proteins which bind preferentially to single-stranded DNA, a low molecular weight protein from Escherichia coli can bind both single-stranded and double-stranded DNA. Rat liver nonhistone proteins have been isolated and analyzed for DNA-binding activity. Labeled nonhistone-bound DNA was hybridized to nitrocellulose bound Eco RI restriction fragments of the rat serum albumin gene. An indirect assay of function for DNA-binding nonhistones has been developed with in vitro initiation assays using partially purified RNA polymerases.
