Recruitment kinetics of DNA repair proteins Mdc1 and Rad52 but not 53BP1 depend on damage complexity
Zeitschrift:
PLoS One
Jahrgang:
7
Heftnummer:
7
Jahr:
2012
Sprache:
Englisch
Stichwörter:
adaptor protein ; carbon ; histone H2AX ; mdc1 protein ; prion protein ; protein 53bp1 ; proton ; Rad52 protein ; unclassified drug, article; carboxy terminal sequence ; controlled study ; disease severity ; DNA damage ; DNA repair ; double stranded DNA break ; ionizing radiation ; kinetics ; laser ; linear energy transfer ; protein analysis ; protein binding ; protein function ; protein metabolism ; protein modification ; protein phosphorylation ; proton radiation ; radiation dose ; recruitment kinetics, Cell Line, Tumor ; DNA Damage ; DNA Repair ; Humans ; Intracellular Signaling Peptides and Proteins ; Kinetics ; Nuclear Proteins ; Rad52 DNA Repair and Recombination Protein ; Trans-Activators ; Ultraviolet Rays «
adaptor protein ; carbon ; histone H2AX ; mdc1 protein ; prion protein ; protein 53bp1 ; proton ; Rad52 protein ; unclassified drug, article; carboxy terminal sequence ; controlled study ; disease severity ; DNA damage ; DNA repair ; double stranded DNA break ; ionizing radiation ; kinetics ; laser ; linear energy transfer ; protein analysis ; protein binding ; protein function ; protein metabolism ; protein modification ; protein phosphorylation ; proton radiation ; ra... »
Abstract:
The recruitment kinetics of double-strand break (DSB) signaling and repair proteins Mdc1, 53BP1 and Rad52 into radiation-induced foci was studied by live-cell fluorescence microscopy after ion microirradiation. To investigate the influence of damage density and complexity on recruitment kinetics, which cannot be done by UV laser irradiation used in former studies, we utilized 43 MeV carbon ions with high linear energy transfer per ion (