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Molecular basis for modulation of biological function by alternate splicing of the Wilms' tumor suppressor protein

Academic Article
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Overview

authors

  • Laity, J. H.
  • Dyson, Jane
  • Wright, Peter

publication date

  • October 2000

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Alternate splicing, leading to the insertion of the tripeptide KTS in the linker between the third and fourth C(2)H(2) zinc fingers, changes both the DNA-binding function and the subnuclear localization of the Wilms' tumor suppressor protein (WT1). We have used NMR relaxation experiments to determine the molecular basis for the differing DNA recognition properties of the WT1-KTS and WT1+KTS isoforms. Our results show that the KTS insertion increases the flexibility of the linker between fingers 3 and 4 and abrogates binding of the fourth zinc finger to its cognate site in the DNA major groove. This represents a mechanism whereby a single zinc-finger gene can be used, through alternate splicing, to fulfill different functions in the cell.

subject areas

  • Alternative Splicing
  • Amino Acid Sequence
  • Base Sequence
  • DNA
  • DNA Primers
  • DNA-Binding Proteins
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Transcription Factors
  • WT1 Proteins
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Identity

PubMed Central ID

  • PMC17272

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.97.22.11932

PubMed ID

  • 11050227
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Additional Document Info

start page

  • 11932

end page

  • 11935

volume

  • 97

issue

  • 22

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