Binding specificity of T4 DNA polymerase to RNA

Autor:	A R, Pavlov, J D, Karam
Rok vydání:	1994
Předmět:	Viral Proteins Base Sequence Molecular Sequence Data Nucleic Acid Conformation RNA DNA-Directed DNA Polymerase Protein Binding Substrate Specificity
Zdroj:	The Journal of biological chemistry. 269(17)
ISSN:	0021-9258
Popis:	Bacteriophage T4 DNA polymerase, product of phage gene 43 (gp43), is a multifunctional DNA-binding protein and a key component of the phage DNA replicase. It is also an RNA-binding protein that selectively recognizes a site on its mRNA (the translational operator) and represses its own translation. We examined the ability of the protein to discriminate between DNA and RNA by using a gel mobility shift assay with defined RNA and DNA substrates. A higher affinity to RNA as compared with DNA (about 100-fold) was observed in assays that utilized synthetic DNA and in vitro transcribed RNA substrates bearing the T4 gene 43 translational operator sequence. The replacement of thymine with uracil in the synthetic DNA did not improve binding. The results suggest that the protein's selectivity for RNA is based in structure (intramolecular interactions) specific to the ribonucleotide sequence of the operator. Competition studies suggest that the protein determinants for RNA and DNA recognition are only partially overlapping.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::13b30e5f9e63ebdf01070ac03939d691 https://pubmed.ncbi.nlm.nih.gov/7513697 Zobrazit plný text záznamu