A novel DNA-binding motif shares structural homology to DNA replication and repair nucleases and polymerases.
A novel class of DNA-binding domains has been established from at least sixteen recently identified DNA-binding proteins. The three-dimensional structure of one of these domains, Mrf-2, has been solved using NMR methods. This structure is significantly different from known DNA-binding domain structures. The mechanism of DNA recognition by this motif has been suggested based on conserved residues, surface electrostatic potentials and chemical shift changes. This new DNA-binding motif shares structural homology with T4 RNase H, E. coli endonuclease III and Bacillus subtilis DNA polymerase I. The structural homology suggests a mechanism for substrate recognition by these enzymes.
Yuan
Y C
YC
Division of Immunology, Beckman Research Institute of the City of Hope, Duarte, California 91010-0269, USA.
Whitson
R H
RH
Liu
Q
Q
Itakura
K
K
Chen
Y
Y
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology; D017122:Bacteriophage T4 / Q000201:enzymology; D017124:Conserved Sequence / Q000235:genetics; D018360:Crystallography, X-Ray; D004256:DNA Polymerase I / Q000737:chemistry*; D004260:DNA Repair; D004261:DNA Replication; D004268:DNA-Binding Proteins / Q000737:chemistry*; D043224:Deoxyribonuclease (Pyrimidine Dimer); D004706:Endodeoxyribonucleases / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins; D016914:Ribonuclease H / Q000737:chemistry*; D016415:Sequence Alignment; D014157:Transcription Factors / Q000737:chemistry*
D004268:DNA-Binding Proteins; D011993:Recombinant Fusion Proteins; D014157:Transcription Factors; D004256:DNA Polymerase I; D004706:Endodeoxyribonucleases; D043224:Deoxyribonuclease (Pyrimidine Dimer); D016914:Ribonuclease H