Mammalian SMC3 C-terminal and coiled-coil protein domains specifically bind palindromic DNA, do not block DNA ends, and prevent DNA bending
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
Abstract
The C-terminal domains of yeast structural maintenance of chromosomes (SMC) proteins were previously shown to bind double-stranded DNA, which generated the idea of the antiparallel SMC heterodimer, such as the SMC1/3 dimer, bridging two DNA molecules. Analysis of bovine SMC1 and SMC3 protein domains now reveals that not only the C-terminal domains, but also the coiled-coil region, binds DNA, while the N terminus is inactive. Duplex DNA and DNA molecules with secondary structures are highly preferred substrates for both the C-terminal and coiled-coil domains. Contrasting other cruciform DNA-binding proteins like HMG1, the SMC3 C-terminal and coiled-coil domains do not bend DNA, but rather prevent bending in ring closure assays. Phosphatase, exonuclease, and ligase assays showed that neither domain renders DNA ends inaccessible for other enzymes. These observations allow modifications of models for SMC-DNA interactions.
Details
Original language | English |
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Pages (from-to) | 38216-24 |
Number of pages | 9 |
Journal | The Journal of biological chemistry |
Volume | 274 |
Issue number | 53 |
Publication status | Published - 31 Dec 1999 |
Peer-reviewed | Yes |
External IDs
Scopus | 0033621490 |
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Keywords
Keywords
- Animals, Base Sequence, Cattle, Cell Cycle Proteins/chemistry, Chromosomal Proteins, Non-Histone/chemistry, DNA/chemistry, DNA Primers, DNA-Binding Proteins/chemistry, Nucleic Acid Conformation, Recombinant Proteins/chemistry