Submitted by alp2017 on April 24, 2015 - 10:51am
| Title | A DNA-binding protein from Ustilago maydis prefers duplex DNA without chain interruptions. |
| Publication Type | Journal Article |
| Year of Publication | 1983 |
| Authors | Rusche JR, Holloman WK |
| Journal | Mol Cell Biol |
| Volume | 3 |
| Issue | 4 |
| Pagination | 605-12 |
| Date Published | 1983 Apr |
| ISSN | 0270-7306 |
| Keywords | Binding Sites, DNA Helicases, DNA, Satellite, DNA-Binding Proteins, Fungi, Protein Binding, Structure-Activity Relationship |
| Abstract | Using a nitrocellulose filter binding assay, we have partially purified a protein from mitotic cells of Ustilago maydis that binds preferentially to covalently closed circular duplex DNA. DNA containing single- or double-strand breaks is bound poorly by the protein. Once formed, the DNA-protein complex is stable, resisting dissociation in high salt. However, when a DNA strand is broken, the complex appears to dissociate. The protein binds equally well to form I DNA of phi X174 or the plasmid pBR322, but has a higher affinity for a hybrid plasmid containing a cloned region of Drosophila melanogaster satellite DNA. |
| Alternate Journal | Mol. Cell. Biol. |
| PubMed ID | 6304499 |
| PubMed Central ID | PMC368576 |
| Grant List | GM 27103 / GM / NIGMS NIH HHS / United States |