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USP1 deubiquitinates hsFANCD2-Ub. 8 / 8
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"With the substrates purified (Fig 2C), we assessed whether hsFANCD2-Ub, hsFANCI-Ub, or hsPCNA-Ub is directly deubiquitinated by USP1–UAF1 in vitro."
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"This is in contrast to USP1 , which is able to deubiquitinate hsFANCD2-Ub at sub-stoichiometric concentrations (Fig 3C)."
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"To determine whether the N-terminus dependence of hsFANCD2-Ub deubiquitination by USP1 was due to possible post-translational modifications in eukaryotic cells, we also expressed and purified USP1 and USP1 from E. coli and tested their activity (Fig S3)."
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"Whereas USP1 is able to deubiquitinate some of the hsFANCD2-Ub in the presence of both DNA and hsFANCI, a portion of hsFANCD2-Ub and hsFANCI-Ub remains resistant to deubiquitination (Fig 7A), consistent with the recent findings using frog substrates (32)."
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"As shown, USP1 –UAF1 readily deubiquitinates hsFANCD2-Ub, hsFANCI-Ub, and hsPCNA-Ub (Fig 3A)."
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"Surprisingly, USP1 –UAF1 is unable to deubiquitinate hsFANCD2-Ub and there is slower activity on hsPCNA-Ub at early time points (Fig 3A), indicating the catalytic domain is not sufficient despite the catalytic domain being active on other substrates including hsFANCI-Ub."
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"Interestingly, when DNA is removed, all of the hsFANCD2-Ub and hsFANCI-Ub is deubiquitinated by USP1 –UAF1; in contrast, USP1 –UAF1 and USP1 –UAF1 do not deubiquitinate hsFANCD2-Ub (Fig 7A)."
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"The recombinant USP1 is able to fully deubiquitinate hsFANCD2-Ub, hsFANCI-Ub, and hsPCNA-Ub at sub-stoichiometric concentrations, in a UAF1-dependent manner (Fig 2D)."
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