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Structure of a Complex of E. coli DNA Polymerase III ε Subunit with Phage P1 Homolog of θ
Author(s) -
KIRBY THOMAS W,
Pedersen Lars,
Harvey Scott,
Perrino Fred W,
London Robert E
Publication year - 2006
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.20.5.lb59-b
Subject(s) - dna polymerase , polymerase , dna polymerase i , exonuclease , protein subunit , specificity factor , microbiology and biotechnology , dna clamp , bacteriophage , biology , dna replication , proofreading , chemistry , dna , genetics , escherichia coli , gene , rna dependent rna polymerase , polymerase chain reaction , reverse transcriptase
When bacteriophage P1 infects E. coli it uses the bacterial DNA Polymerase III holoenzyme to effect replication. The phage genome encodes a homolog of one of the subunits of the DNA Polymerase III core named HOT (homolog of θ ). The function of θ is not known but it binds to the ε subunit (proofreading exonuclease) and not to the α subunit (polymerase) to create the core, a linear α‐ε‐ θ unit. HOT can effectively substitute for θ in E. coli but it causes some changes in the core as evidenced by differences in the mutator effects of certain dnaQ mutants (amino acid changes in the ε subunit). NMR spectroscopy has been used to determine the structures of HOT and of θ , while X‐ray crystallography has yielded the structure of the N‐terminal domain of ε (ε186), which contains the binding site for θ but not the binding site for α. In order to better understand how HOT affects ε, we are using structural biology techniques to characterize the interaction between HOT and ε186.