BMB 495 Weinreich report paper

BMB 495 Weinreich report paper - BMB 495 3/8/08 Summary...

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BMB 495 3/8/08 Summary Report for 3/11 – Weinreich Title and Journal Reference: Erzberger, Jan P., Melissa L. Mott, and James M. Berger. "Structural basis for ATP- dependent DnaA assembly and replication-origin remodeling." Nature Structural 13.8 (2006): 676-83. Hypothesis: Structural analysis of ATP-bound DnaA will reveal significant details surrounding the mechanism by which DnaA is activated by the binding of ATP and oligimerized to drive replication-origin remodeling in prokaryotes. Background/Significance: The structure and function of DnaA, an important member of the AAA+ family of proteins, has long been studied by researchers. It is characterized as a protein (more specifically, a replication initiation factor) that is vital to the unwinding and replication of DNA in prokaryotes. It has been found that DnaA is highly conserved in all bacteria, despite the vast variation of bacterial DnaA box arrangements. When ATP binds to DnaA in its monomeric state, the protein undergoes a conformational change resulting in an oligimeric complex that can remodel replication origins and initiate the start of the DNA replication process. While it has been known for some time that DnaA controls DNA replication in prokaryotes, the details of this process on a molecular level have thus far eluded scientists. The research presented in this paper by
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BMB 495 Weinreich report paper - BMB 495 3/8/08 Summary...

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