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Domain Structure and Protein Interactions of the Silent Information Regulator Sir3 Revealed by Screening a Nested Deletion Library of Protein Fragments
- Source :
- Journal of Biological Chemistry. 281:20107-20119
- Publication Year :
- 2006
- Publisher :
- Elsevier BV, 2006.
-
Abstract
- Transcriptional silencing in yeast is mediated by the interactions of silent information regulator (Sir) proteins with chromatin and with one another. The stable association of Sir3 with Sir4 is mediated by a C-terminal region of Sir3 that has additional functions including the dimerization of Sir3. We have developed a simple, robust expression screening methodology that allows for the unbiased identification of functional protein domains expressed from nested-deletion libraries of full-length genes. Using these methodologies, Sir3 dimerization was shown to be mediated by two separate domains. One of these domains also binds cooperatively to the C-terminal coiled-coil motif of Sir4 and dimerization further increases the affinity of Sir3 for Sir4. The resulting Sir3-Sir4 complexes form progressively higher order assemblies with increasing protein concentration, with implications for the mechanism of gene silencing.
- Subjects :
- Saccharomyces cerevisiae Proteins
Protein domain
Regulator
Saccharomyces cerevisiae
Computational biology
Biology
Biochemistry
Protein–protein interaction
Gene silencing
Gene Silencing
DNA, Fungal
Molecular Biology
Gene
Silent Information Regulator Proteins, Saccharomyces cerevisiae
Sequence Deletion
Genetics
Binding Sites
Base Sequence
Cell Biology
Recombinant Proteins
Yeast
Chromatin
Kinetics
Protein Subunits
Oligodeoxyribonucleotides
Dimerization
Protein concentration
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 281
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry
- Accession number :
- edsair.doi.dedup.....06b0945686a6afcd549d307f07b5b9ef