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[ subject:"Chemistry, Biochemistry." ]
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The unique role of polymerase mu in ...
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The University of North Carolina at Chapel Hill., Biochemistry and Biophysics.
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The unique role of polymerase mu in nonhomologous end joining.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
The unique role of polymerase mu in nonhomologous end joining./
作者:
Davis, Bryan Joseph.
面頁冊數:
71 p.
附註:
Adviser: Dale A. Ramsden.
Contained By:
Dissertation Abstracts International69-11B.
標題:
Chemistry, Biochemistry. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3331008
ISBN:
9780549881070
The unique role of polymerase mu in nonhomologous end joining.
Davis, Bryan Joseph.
The unique role of polymerase mu in nonhomologous end joining.
- 71 p.
Adviser: Dale A. Ramsden.
Thesis (Ph.D.)--The University of North Carolina at Chapel Hill, 2008.
Nonhomologous end-joining (NEHJ) has the challenge of repairing DNA double strand breaks (DSBs) without using an intact template molecule to instruct synthesis. NHEJ solves this problem in part by recruiting polymerases from the pol X family to fill gaps that are present at some DSBs. If a gap has some complementary bases, multiple pol X family members can participate in NHEJ, but only pol mu is able to fill the gap if the DNA ends are noncomplementary. I determined that pol mu fills these gaps in a template-directed way, successfully using as template a DNA strand that is not annealed to the primer. My results show pol mu is able to do this because it interacts with DNA on both sides of the gap. Further, I demonstrate that the polymerase is most efficient when it participates in such an end-bridging complex. I then determined the roles of two amino acid residues in pol mu's activity on noncomplementary ends. As a similar residue does in TdT, H329 helps pol mu stabilize the incoming nucleotide when the template strand does not. However, unlike TdT, I show pol mu is not promiscuously template independent. I argue this is in part because pol mu also possesses an element of the more canonical template dependent pol X family members. R175 is part of the 8 kDa domain and helps position the template opposite the primer terminus through an interaction with the downstream phosphate. Pol mu is the only polymerase that has both of these elements and the combination confers the unique ability to fill gaps between noncomplementary ends.
ISBN: 9780549881070Subjects--Topical Terms:
1017722
Chemistry, Biochemistry.
The unique role of polymerase mu in nonhomologous end joining.
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Nonhomologous end-joining (NEHJ) has the challenge of repairing DNA double strand breaks (DSBs) without using an intact template molecule to instruct synthesis. NHEJ solves this problem in part by recruiting polymerases from the pol X family to fill gaps that are present at some DSBs. If a gap has some complementary bases, multiple pol X family members can participate in NHEJ, but only pol mu is able to fill the gap if the DNA ends are noncomplementary. I determined that pol mu fills these gaps in a template-directed way, successfully using as template a DNA strand that is not annealed to the primer. My results show pol mu is able to do this because it interacts with DNA on both sides of the gap. Further, I demonstrate that the polymerase is most efficient when it participates in such an end-bridging complex. I then determined the roles of two amino acid residues in pol mu's activity on noncomplementary ends. As a similar residue does in TdT, H329 helps pol mu stabilize the incoming nucleotide when the template strand does not. However, unlike TdT, I show pol mu is not promiscuously template independent. I argue this is in part because pol mu also possesses an element of the more canonical template dependent pol X family members. R175 is part of the 8 kDa domain and helps position the template opposite the primer terminus through an interaction with the downstream phosphate. Pol mu is the only polymerase that has both of these elements and the combination confers the unique ability to fill gaps between noncomplementary ends.
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