| Structural Studies of DNA Replication Proteins
Xiangpeng Kong Ph.D.
Associate Professor
Department of Biochemistry (Skirball) Skirball Institute Program of Structural Biology |
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| Research Summary |
| Using crystallographic methods, we study chromosomal DNA replication by determining three-dimensional protein structures of its machinery. We are particularly interested in the role of DNA polymerases. These unique molecules are involved in chromosomal replication and can polymerize thousands of nucleotides in one continuous process. This remarkable output is usually achieved by using the so-called processivity factor proteins. The three-dimensional structure of the processivity factor (b subunit) of Escherichia coli DNA polymerase III holoenzyme was recently determined. The structure shows that the dimer of the subunit forms a highly symmetrical closed ring with a large hole in the center. It can encircle and fasten the holoenzyme onto duplex DNA tightly but nonspecifically, hence the name, DNA sliding clamp. We continue to study the properties of the clamp and its interaction with other subunits of the holoenzyme by determining various mutants of the beta subunit. We are also conducting crystallographic studies of other DNA replication proteins, especially those involved in the initiation of DNA replication.
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| Related Images |
Image 1 | We are also conducting crystallographic studies of other DNA replication proteins, especially those involved in the initiation of DNA replication. | | |
| Research Information |
Research Interests | Structural Studies of DNA Replication Proteins | Research Keywords | crystallographic studies, DNA polymerases, DNA replication proteins, holoenzyme |
