The bond in the bacteriophage øX174 gene A protein-DNA complex is a tyrosyl-5'-phosphate ester

Autor: H.S. Jansz, G. H. Veeneman, J. H. Van Boom, H.A.A.M. van Teeffelen, P.D. Baas, A.D.M. van Mansfeld
Jazyk: angličtina
Předmět:
Zdroj: FEBS Letters. (2):351-356
ISSN: 0014-5793
DOI: 10.1016/0014-5793(84)80804-2
Popis: The bacteriophage øX174 gene A protein cleaves the viral strand of the double-stranded replicative form (RF) DNA of the phage at a specific site, the origin. It leaves a free 3'-OH at nucleotide 4305 (G) of the øx DNA sequence and binds covalently to the DNA. The nature and position of the covalent bond have been determined using the octadecadesoxyribonucleotide CAACTTG[32P]ATATTAATAAC. This octadecamer, which corresponds to nucleotides 4299–4316 of øX viral DNA, is cleaved by gene A protein. Gene A protein is bound to the labelled phosphate via a tyrosyl residue, indicating that binding occurs to the nucleotide corresponding to 4306 (A) of the øX viral DNA strand.Bacteriophage øX174Gene A proteinDNA replicationProtein-DNA complexSynthetic oligonucleotideTyrosyl-5'-phosphate ester
Databáze: OpenAIRE