Journal article
Isolation of Drosophila proteins that bind selectively to left-handed Z-DNA
Proceedings of the National Academy of Sciences of the United States of America, Vol.79(24 I), pp.7729-7733
1982
DOI: 10.1073/pnas.79.24.7729
PMID: 6296848
Abstract
An affinity column for isolating Z-DNA binding proteins was made by attaching brominated poly(dG-dC) to Sephadex. Proteins from Drosophila nuclei were prepared and those that could bind to Escherichia coli B-DNA were removed from the solution. The remaining proteins were passed over the Z-DNA affinity column and then eluted with NaCl. Using both direct and competitive filter binding assays, we found that the eluted proteins bind to brominated poly(dG-dC) (Z-DNA) and poly(dG-m5dC) but not to poly(dG-dC) (B-DNA), native or denatured E. coli or calf thymus DNA, or brominated oligonucleotides. The proteins also bind to negatively supercoiled plasmids carrying Z-DNA sequences but not to relaxed or linearized plasmids in which the Z-DNA conformation is no longer present. Gel analysis reveals a mixture of several large proteins up to approximately 150,000 daltons.
Details
- Title: Subtitle
- Isolation of Drosophila proteins that bind selectively to left-handed Z-DNA
- Creators
- Alfred NordheimPaul TesserFernando AzorinYoung Ha KwonAchim MöllerAlexander Rich
- Resource Type
- Journal article
- Publication Details
- Proceedings of the National Academy of Sciences of the United States of America, Vol.79(24 I), pp.7729-7733
- DOI
- 10.1073/pnas.79.24.7729
- PMID
- 6296848
- NLM abbreviation
- Proc Natl Acad Sci U S A
- ISSN
- 0027-8424
- eISSN
- 1091-6490
- Language
- English
- Date published
- 1982
- Academic Unit
- Ophthalmology and Visual Sciences
- Record Identifier
- 9983980391202771
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