Open AccessEvolutionary conservation of DNA polymerase beta structure.
Author(s) -
Lucy M.S. Chang,
Paolo Plevani,
F. J. Bollum
Publication year - 1982
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.79.3.758
Subject(s) - polymerase , dna polymerase , biology , microbiology and biotechnology , dna polymerase beta , dna , gel electrophoresis , biochemistry , antiserum , enzyme , dna clamp , polymerase chain reaction , genetics , gene , dna repair , reverse transcriptase , antibody , base excision repair
An immunological procedure that uses antiserum against homogeneous calf thymus DNA polymerase beta to detect immunoreactive peptides on NaDodSO4/polyacrylamide gel electrophoresis demonstrates a high degree of conservation of protein sequence and molecular weight for this enzyme, from parastic protozoans to man. By renaturation of DNA polymerase activity in situ after electrophoresis, the enzymatically active peptides are shown to correspond to the immunoreactive peptides. The persistence of sequence and molecular weight for the catalytic peptide of DNA polymerase beta through eons of evolutionary time suggests an essential role for this enzyme in DNA metabolism of complex cells.