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Initial Crystallography of a Phage DNA Kinase
Author(s) -
Gnann Andrew,
Weigele Peter,
Dowling Daniel
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.lb89
Subject(s) - dna , biology , phagemid , nucleic acid , biochemistry , thymine , restriction enzyme , dna polymerase , bacteriophage , microbiology and biotechnology , chemistry , gene , escherichia coli
Enzymes capable of selectively modifying DNA comprise an attractive field of research. Modified nucleotides are involved in many biological phenomena ranging from differential gene expression to packaging of nucleic acids in viral capsids. Interesting examples of DNA modification have been found in bacteriophages of gram‐negative bacteria, which use hypermodification of DNA bases to prevent recognition of viral DNA by host restriction endonucleases during infection. Hypermodification of 5‐hydroxymethyl‐2′‐deoxyuridine, a noncanonical DNA base incorporated in some phage genomes in place of thymine, begins with phosphorylation of the C5 hydroxymethyl group. Structural information about the kinase responsible for this phosphorylation reaction will shed light on a largely unstudied class of DNA kinases that can modify duplex DNA (dsDNA) at the major groove. These enzymes may prove useful as molecular biological tools targeting DNA modification states in the DNA polymer. To acquire high‐resolution structural information, we are employing protein crystallography. Here we report biochemical characterization and crystallization of the kinase involved in this bacteriophage DNA hypermodification.