Sequence discrimination by alternatively spliced isoforms of a DNA binding zinc finger domain
- 25 September 1992
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 257 (5078), 1951-1955
- https://doi.org/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.Keywords
This publication has 19 references indexed in Scilit:
- Developmental switch of CREM function during spermatogenesis: from antagonist to activatorNature, 1992
- Interaction of TFIID in the minor groove of the TATA elementCell, 1991
- Zinc Finger-DNA Recognition: Crystal Structure of a Zif268-DNA Complex at 2.1 ÅScience, 1991
- A naturally occurring truncated form of FosB that inhibits Fos/Jun transcriptional activityCell, 1991
- Binding site selection analysis of protein-DNA interactions via solid phase sequencing of oligonucleotide mixturesNucleic Acids Research, 1991
- Base sequence discrimination by zinc-finger DNA-binding domainsNature, 1991
- Differences and Similarities in DNA-Binding Preferences of MyoD and E2A Protein Complexes Revealed by Binding Site SelectionScience, 1990
- A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteinsCell, 1989
- Inhibition of thyroid hormone action by a non-hormone binding c-erbA protein generated by alternative mRNA splicingNature, 1989
- Structure of the DNA-Eco RI Endonuclease Recognition Complex at 3 Å ResolutionScience, 1986