Functional interaction between hMutSα and wild-type and mutant hMYH proteins

<p><b>Copyright information:</b></p><p>Taken from "Functional characterization of two human MutY homolog (hMYH) missense mutations (R227W and V232F) that lie within the putative hMSH6 binding domain and are associated with hMYH polyposis"</p><p>Nucleic Acids Research 2005;33(2):597-604.</p><p>Published online 26 Jan 2005</p><p>PMCID:PMC548354.</p><p>© The Author 2005. Published by Oxford University Press. All rights reserved</p> The glycosylase assay was performed as in , except that the reactions contained different amounts of hMYH proteins and 0.25 or 2 nM of hMutSα. Lane 1–3, reactions contained 10 nM of wild-type hMYH with 0, 0.25 and 2 nM of hMutSα, respectively; lanes 4–6, reactions contained 109 nM of hMYH(R227W); and lanes 7–9, reactions contained 40 nM of hMYH(V232F). The arrows indicate the intact DNA substrate and nicked product

Functional characterization of two human MutY homolog (hMYH) missense mutations (R227W and V232F) that lie within the putative hMSH6 binding domain and are associated with hMYH polyposis-0

<p><b>Copyright information:</b></p><p>Taken from "Functional characterization of two human MutY homolog (hMYH) missense mutations (R227W and V232F) that lie within the putative hMSH6 binding domain and are associated with hMYH polyposis"</p><p>Nucleic Acids Research 2005;33(2):597-604.</p><p>Published online 26 Jan 2005</p><p>PMCID:PMC548354.</p><p>© The Author 2005. Published by Oxford University Press. All rights reserved</p