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Shlomo Eisenberg

Professor of Molecular, Microbial and Structural Biology
seisenberg@nso2.uchc.edu

Shlomo Eisenberg
Areas of Interest

Our long-term goal is to understand the biochemical mechanism responsible for the initiation and regulation of replication of a eukaryotic chromosome. DNA replication is one of the fundamental processes in a living cell. We are studying DNA replication using the yeast S. cerevisiae as model system.

Although the genes involved in the initiation of replication of a S. cerevisiae chromosome have been identified, the biochemical process of the initiation has not been elucidated. In order to understand how DNA replication is initiated at a yeast replication origin, we are aiming to reconstitute in vitro a functional replication initiation complex. Recent studies in our laboratory dealt with the architecture of yeast replication origins and origin binding proteins. We have recently reconstituted in vitro the assembly of a stable and specific multiprotein complex at an origin of replication. The assembly of this complex involved purified Abf1p, purified Hdfp (the yeast homologue of the mammalian Ku) and Orcp. Currently we are engaged in the in vitro reconstitution of the MCM complex, a protein composed of six independent subunits, and essential for the initiation and elongation phases of the replication of yeast chromosomes.

Selected Publications

Shlomo Eisenberg and Bik Tye. (2004) In vitro assembly of the MCM complex. In preparation

Santanu Raychaudhuri, Randy Byers, Todd Upton and Shlomo Eisenberg. (1997) Functional analysis of a replication origin from Saccharomyces cerevisiae: Identification of a new replication enhancer. Nucleic Acids Research 25, 5057-5064.

Steven Wiltshire, Santanu Raychaudhuri and Shlomo Eisenberg. (1997) An Abf1p C-terminal region lacking transcriptional activation potential stimulates a yeast origin of replication. Nucleic Acids Research. 25, 4250-4256.

Nader Shakibai, Vijay Kumar and Shlomo Eisenberg. (1996) The Ku-like protein from Saccharomyces cerevisiae is required in vitro for the assembly of a stable multiprotein complex at a eukaryotic origin of replication. Proc. Natl. Acad. Sci. 93: 11569-11574.

  
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