Purification of a yeast protein that binds to origins of DNA replication and a transcriptional silencer.
- 1 April 1988
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 85 (7) , 2120-2124
- https://doi.org/10.1073/pnas.85.7.2120
Abstract
Two factors that interact specifically with the chromosomal replicator, autonomously replicating sequence 1 (ARS1), were identified in whole-cell yeast extracts. One of these proteins, ARS binding factor I (ABF-I), was purified to homogeneity as a polypeptide of 135 kDa. ABF-I binds within a region previously shown to be essential for the function of ARS1 when yeast are grown under certain nutritional conditions, and deletion analysis presented here suggests that the ARS1 domain containing the ABF-I-binding site, domain B, is a complex element composed of at least two subdomains. ABF-I also binds within an ARS at the HMR silent mating locus. This ARS functions as a cis-acting transcriptional silencer, and the ABF-I-binding site within this ARS is important for both ARS and silencer function.This publication has 40 references indexed in Scilit:
- A yeast silencer contains sequences that can promote autonomous plasmid replication and transcriptional activationCell, 1987
- The localization of replication origins on ARS plasmids in S. cerevisiaeCell, 1987
- The in vivo replication origin of the yeast 2μm plasmidCell, 1987
- RepA and DnaA proteins are required for initiation of R1 plasmid replication in vitro and interact with the oriR sequence.Proceedings of the National Academy of Sciences, 1987
- A Promoter with an Internal Regulatory Domain Is Part of the Origin of Replication in BPV-1Science, 1987
- A cellular DNA-binding protein that activates eukaryotic transcription and DNA replicationCell, 1987
- Fine-structure analysis of the DNA sequence requirements for autonomous replication of Saccharomyces cerevisiae plasmids.Molecular and Cellular Biology, 1986
- Purification of a cellular, double-stranded DNA-binding protein required for initiation of adenovirus DNA replication by using a rapid filter-binding assay.Molecular and Cellular Biology, 1986
- Coupling of glycosaminoglycans to agarose beads (Sepharose 4B)Biochemical Journal, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970