Footprinting of protein interactions by tritium labeling.
A new footprinting method for mapping protein interactions has been developed, using tritium as a radioactive label. As residues involved in an interaction are less labeled when the complex is formed, they can be identified via comparison of the tritium incorporation of each residue of the bound protein with that of the unbound one. Application of this footprinting method to the complex formed by the histone H3 fragment H3(122-135) and the protein hAsf1A(1-156) afforded data in good agreement with NMR results.
Mousseau
Guillaume
G
IBITECS, CNRS CEA, F-91191 Gif-sur-Yvette, France.
Raffy
Quentin
Q
Thomas
Olivier P
OP
Agez
Morgane
M
Thai
Robert
R
Renault
Jean Philippe
JP
Pin
Serge
S
Ochsenbein
Françoise
F
Cintrat
Jean-Christophe
JC
Rousseau
Bernard
B
D000595:Amino Acid Sequence; D004526:Efficiency; D006657:Histones / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D007553:Isotope Labeling / Q000379:methods*; D008954:Models, Biological; D019906:Nuclear Magnetic Resonance, Biomolecular; D009707:Nucleosomes / Q000737:chemistry / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D023302:Protein Footprinting / Q000379:methods*; D025941:Protein Interaction Mapping / Q000379:methods; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D012680:Sensitivity and Specificity; D014316:Tritium
D006657:Histones; D009707:Nucleosomes; D010446:Peptide Fragments; D011506:Proteins; D014316:Tritium