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Faculty

Shlomo Eisenberg
Professor of Molecular, Microbial & Structural Biology
seisenberg@nso2.uchc.edu
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. |