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DNA damage can cause the process of DNA replication to stall and this can lead to dissociation of the DNA replication enzymes from the DNA. In bacteria, a protein called PriA recognizes this, unwinds a portion of duplex DNA at the site where replication stalled, and reloads the replication enzymes to restart DNA replication. PriA has multiple structural domains that are closely associated with one another to give rise to a compact globular protein. The winged helix domain, however, is connected to the remainder of the protein by a long, flexible portion of polypeptide, akin to a tether. I examined the significance of the winged helix domain’s long, flexible tether by lengthening it at its C-terminal end even further. I hypothesized that this would alter its DNA unwinding capability. Through a helicase assay I observed that lengthening the C-terminal tether did not change its capability to unwind duplex DNA.
Matthew E Lopper
Primary Advisor's Department
Stander Symposium poster
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Kirk, Sydney E., "Mutant PriA C-Tev ML346 and its Unwinding DNA Capabilities" (2016). Stander Symposium Posters. 735.
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