User:Scott H. Vanson/Sandbox 1
From Proteopedia
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(New page: ==DNA Polymerase θ== <StructureSection load='4x0p' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for your page '''Scott H. Vanson/Sandbox 1...) |
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==DNA Polymerase θ== | ==DNA Polymerase θ== | ||
| - | <StructureSection load='4x0p' size='340' side='right' caption=' | + | <StructureSection load='4x0p' size='340' side='right' caption='Polymerase θ polymerase domain bound to DNA''> |
This is a default text for your page '''Scott H. Vanson/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page '''Scott H. Vanson/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
== General Description == | == General Description == | ||
| - | Human polymerase θ (pol θ) is large, 290kD enzyme consisting of three distinct domains (1,2). An N-terminal helicase-like domain, whose exact cellular functions are a topic of on-going debate and research, is linked to a C-terminal polymerase domain by a large and disordered central region (2). | + | Human polymerase θ (pol θ) is large, 290kD enzyme consisting of three distinct domains (1,2). An N-terminal helicase-like domain, whose exact cellular functions are a topic of on-going debate and research (3,4), is linked to a C-terminal, family A DNA polymerase domain by a large and disordered central region (2). Notably, pol θ is the only known human polymerase to contain a polymerase and helicase domain in one molecule (5). The focus of this page is the polymerase domain. |
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| + | Pol θ is thought to promote overall genomic stability by performing several distinct cellular functions. The primary role of the enzyme is to repair of double-stranded DNA breaks as the key enzyme in an error-prone non-homologous end-joining pathway called alternative end-joining (6) or theta-mediated end-joining. | ||
== Structural Highlights == | == Structural Highlights == | ||
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</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
| + | 1. Yousefzadeh MJ, Wood RD. DNA polymerase POLQ and cellular defense against DNA damage. DNA Repair (Amst). 2013; 12:1–9. [PubMed: 23219161] | ||
| + | 2. Seki M, Marini F, Wood RD. POLQ (Pol theta), a DNA polymerase and DNA-dependent ATPase in human cells. Nucleic Acids Res. 2003; 31:6117–6126. [PubMed: 14576298] | ||
| + | 3. Sfeir RPA | ||
| + | 4. Pomerantz Helicase | ||
| + | 5. Zahn | ||
| + | 6. Yousefzadeh MJ, et al. Mechanism of Suppression of Chromosomal Instability by DNA Polymerase POLQ. PLoS Genet. 2014; 10:e1004654. [PubMed: 25275444] | ||
<references/> | <references/> | ||
Revision as of 16:17, 28 April 2018
DNA Polymerase θ
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References
1. Yousefzadeh MJ, Wood RD. DNA polymerase POLQ and cellular defense against DNA damage. DNA Repair (Amst). 2013; 12:1–9. [PubMed: 23219161] 2. Seki M, Marini F, Wood RD. POLQ (Pol theta), a DNA polymerase and DNA-dependent ATPase in human cells. Nucleic Acids Res. 2003; 31:6117–6126. [PubMed: 14576298] 3. Sfeir RPA 4. Pomerantz Helicase 5. Zahn 6. Yousefzadeh MJ, et al. Mechanism of Suppression of Chromosomal Instability by DNA Polymerase POLQ. PLoS Genet. 2014; 10:e1004654. [PubMed: 25275444]
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
