Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:6.5.1.2 (
DNA ligase
)
2,749
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Human Rad51 protein (
HsRad51
) is a homolog of Escherichia coli RecA protein, and functions in DNA repair and recombination. In higher eukaryotes, Rad51 protein is essential for cell viability. The N-terminal region of
HsRad51
is highly conserved among eukaryotic Rad51 proteins but is absent from RecA, suggesting a Rad51-specific function for this region. Here, we have determined the structure of the N-terminal part of
HsRad51
by NMR spectroscopy. The N-terminal region forms a compact domain consisting of five short helices, which shares structural similarity with a domain of endonuclease III, a
DNA repair enzyme
of E. coli. NMR experiments did not support the involvement of the N-terminal domain in
HsRad51
-HsBrca2 interaction or the self-association of
HsRad51
as proposed by previous studies. However, NMR tiration experiments demonstrated a physical interaction of the domain with DNA, and allowed mapping of the DNA binding surface. Mutation analysis showed that the DNA binding surface is essential for double-stranded and single-stranded DNA binding of
HsRad51
. Our results suggest the presence of a DNA binding site on the outside surface of the
HsRad51
filament and provide a possible explanation for the regulation of DNA binding by phosphorylation within the N-terminal domain.
...
PMID:The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR. 1039 Mar 47
