Processivity of nucleic acid unwinding and translocation by helicases |
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| Authors: | Ping Xie |
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| Affiliation: | Key Laboratory of Soft Matter Physics and Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, China |
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| Abstract: | Helicases are a class of enzymes that use the chemical energy of NTP hydrolysis to drive mechanical processes such as translocation and nucleic acid (NA) strand separation. Besides the NA unwinding speed, another important factor for the helicase activity is the NA unwinding processivity. Here, we study the NA unwinding processivity with an analytical model that captures the phenomenology of the NA unwinding process. First, we study the processivity of the non‐hexameric helicase that can unwind NA efficiently in the form of a monomer and the processivity of the hexameric helicase that can unwind DNA effectively, providing quantitative explanations of the available single‐molecule experimental data. Then, we study the processivity of the non‐hexameric helicases, in particular UvrD, in the form of a dimer and compare with that in the form of a monomer. The available single‐molecule and some biochemical data showing that while UvrD monomer is a highly processive single‐stranded DNA translocase it is inactive in DNA unwinding, whereas other biochemical data showing that UvrD is active in both single‐stranded DNA translocation and DNA unwinding in the form of a monomer can be explained quantitatively and consistently. In addition, the recent single‐molecule data are also explained quantitatively showing that constraining the 2B subdomain in closed conformation by intramolecular cross‐linking can convert Rep monomer with a very poor DNA unwinding activity into a superhelicase that can unwind more than thousands of DNA base pairs processively, even against a large opposing force. Proteins 2016; 84:1590–1605. © 2016 Wiley Periodicals, Inc. |
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| Keywords: | helicase monomer helicase dimer DNA unwinding translocation processivity |
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