RNA Binding by the KTS Splice Variants of Wilms' Tumor Suppressor Protein WT1.

ABSTRACT: Wilms' tumor suppressor protein WT1 regulates the expression of multiple genes through binding of the Cys₂-His₂ zinc finger domain to promoter sites. WT1 has also been proposed to be involved in post-transcriptional regulation, by binding to RNA using the same set of zinc fingers. WT1 has two major splice variants, where the Lys-Thr-Ser (KTS) tripeptide is inserted into the linker between the third and fourth zinc fingers. To obtain insights into the mechanism by which the different WT1 splice variants recognize both DNA and RNA, we have determined the solution structure of the WT1 (-KTS) zinc finger domain in complex with a 29mer stem-loop RNA. Zinc fingers 1-3 bind in a widened major groove favored by the presence of a bulge nucleotide in the double-stranded helical

SUBMITTER: Nishikawa T 

PROVIDER: S-EPMC7572782 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature