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Description

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.

Publication Date

4-9-2016

Project Designation

Course Project

Primary Advisor

Matthew E Lopper

Primary Advisor's Department

Chemistry

Keywords

Stander Symposium poster

Disciplines

Arts and Humanities | Business | Education | Engineering | Life Sciences | Medicine and Health Sciences | Physical Sciences and Mathematics | Social and Behavioral Sciences

Comments

This poster reflects research conducted as part of course project designed to give students experience in the research process.

Mutant PriA C-Tev ML346 and its Unwinding DNA Capabilities

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