Sequence discrimination by alternatively spliced isoforms of a DNA binding zinc finger domain

Science. 1992 Sep 25;257(5078):1951-5. doi: 10.1126/science.1290524.

Abstract

Two major developmentally regulated isoforms of the Drosophila chorion transcription factor CF2 differ by an extra zinc finger within the DNA binding domain. The preferred DNA binding sites were determined and are distinguished by an internal duplication of TAT in the site recognized by the isoform with the extra finger. The results are consistent with modular interactions between zinc fingers and trinucleotides and also suggest rules for recognition of AT-rich DNA sites by zinc finger proteins. The results show how modular finger interactions with trinucleotides can be used, in conjunction with alternative splicing, to alter the binding specificity and increase the spectrum of sites recognized by a DNA binding domain. Thus, CF2 may potentially regulate distinct sets of target genes during development.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alternative Splicing*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites
  • DNA-Binding Proteins / metabolism*
  • Drosophila Proteins*
  • Drosophila melanogaster / genetics
  • Hydrogen Bonding
  • Molecular Sequence Data
  • Oligodeoxyribonucleotides / chemistry
  • Oligodeoxyribonucleotides / metabolism
  • Protein Binding
  • Regulatory Sequences, Nucleic Acid*
  • Structure-Activity Relationship
  • Transcription Factors / metabolism*
  • Zinc Fingers*

Substances

  • DNA-Binding Proteins
  • Drosophila Proteins
  • Oligodeoxyribonucleotides
  • Transcription Factors
  • Cf2 protein, Drosophila