ATM Kinase and BLM Helicase: A Regulator and Key Player in Microhomology-Mediated End Joining

Persistent Link:
http://hdl.handle.net/10150/146020
Title:
ATM Kinase and BLM Helicase: A Regulator and Key Player in Microhomology-Mediated End Joining
Author:
Treister, Daniel
Issue Date:
May-2010
Publisher:
The University of Arizona.
Rights:
Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
Abstract:
Microhomology-mediated end joining (MMEJ) is a class of DNA repair used to join DNA ends following a double-strand break (DSB). It represents an unfavorable and error-prone pathway because it results in deletion of nucleotides between microhomologies, as well as the deletion of one microhomology. This study utilized a DNA repair assay to measure degradation prior to end rejoining in nuclear extracts. Our results were consistent with previous studies which found that ATM plays a regulatory role in repressing nuclease degradation of DSB ends and that BLM is a required component in the MMEJ pathway. MMEJ repair products were also found to utilize GC rich microhomologies and preferred sites for rejoining. Variation among extracts from the same cell line suggest that additional trials of the repair assay must be conducted to ensure that the differences in CF, AT, and BLM nuclear extracts are the result of protein composition differences rather than variation in extract preparation.
Type:
text; Electronic Thesis
Degree Name:
B.S.
Degree Level:
bachelors
Degree Program:
Honors College; Biochemistry and Molecular Biophysics
Degree Grantor:
University of Arizona

Full metadata record

DC FieldValue Language
dc.language.isoenen_US
dc.titleATM Kinase and BLM Helicase: A Regulator and Key Player in Microhomology-Mediated End Joiningen_US
dc.creatorTreister, Danielen_US
dc.contributor.authorTreister, Danielen_US
dc.date.issued2010-05-
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.description.abstractMicrohomology-mediated end joining (MMEJ) is a class of DNA repair used to join DNA ends following a double-strand break (DSB). It represents an unfavorable and error-prone pathway because it results in deletion of nucleotides between microhomologies, as well as the deletion of one microhomology. This study utilized a DNA repair assay to measure degradation prior to end rejoining in nuclear extracts. Our results were consistent with previous studies which found that ATM plays a regulatory role in repressing nuclease degradation of DSB ends and that BLM is a required component in the MMEJ pathway. MMEJ repair products were also found to utilize GC rich microhomologies and preferred sites for rejoining. Variation among extracts from the same cell line suggest that additional trials of the repair assay must be conducted to ensure that the differences in CF, AT, and BLM nuclear extracts are the result of protein composition differences rather than variation in extract preparation.en_US
dc.typetexten_US
dc.typeElectronic Thesisen_US
thesis.degree.nameB.S.en_US
thesis.degree.levelbachelorsen_US
thesis.degree.disciplineHonors Collegeen_US
thesis.degree.disciplineBiochemistry and Molecular Biophysicsen_US
thesis.degree.grantorUniversity of Arizonaen_US
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