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Full-Text Articles in Genetics and Genomics
Strand Exchange Protein 1 (Sep1) From Saccharomyces Cerevisiae Does Not Promote Branch Migration In Vitro, Zhaoqing Zhang, Amanda Simons, Vidya Prabhu, Junghuei Chen
Strand Exchange Protein 1 (Sep1) From Saccharomyces Cerevisiae Does Not Promote Branch Migration In Vitro, Zhaoqing Zhang, Amanda Simons, Vidya Prabhu, Junghuei Chen
Amanda Simons
It has been shown in vitro that Saccharomyces cerevisiae strand exchange protein 1 (Sep1) promotes the transfer of one strand of a linear duplex DNA to a homologous single-stranded DNA circle. Sep1 also has an exonuclease active on DNA and RNA. By using exonuclease III-treated linear duplex DNA with various lengths of single-stranded tail as well as Ca2+ to inhibit the exonuclease activity of Sep1, we show that the processivity of exonuclease activity of Sep1 is greater than previously reported. The results in this work also demonstrate that the joint molecule between the linear duplex and single-stranded circle observed from …
Direct Dna Binding Activity Of The Fanconi Anemia D2 Protein, Woo-Hyun Park, Steven Margossian, Andrew Horwitz, Amanda Simons, Alan D'Andrea, Jeffrey Parvin
Direct Dna Binding Activity Of The Fanconi Anemia D2 Protein, Woo-Hyun Park, Steven Margossian, Andrew Horwitz, Amanda Simons, Alan D'Andrea, Jeffrey Parvin
Amanda Simons
It is known that the Fanconi anemia D2 protein is vital for protecting the genome from DNA damage, but what activities this protein has are unknown. In these experiments we purified full-length Fanconi anemia protein D2 (FANCD2), and we found that FANCD2 bound to DNA with specificity for certain structures: double strand DNA ends and Holliday junctions. Proteins containing patient-derived mutations or artificial variants of the FANCD2 protein were similarly expressed and purified, and each variant bound to the Holliday junction DNA with similar affinity as did the wild-type protein. There was no single discrete domain of FANCD2 protein that …
A Unified View Of Base Excision Repair, Karen Almeida, Robert Sobol
A Unified View Of Base Excision Repair, Karen Almeida, Robert Sobol
Karen H Almeida
Base excision repair (BER) proteins act upon a significantly broad spectrum of DNA lesions that result from endogenous and exogenous sources. Multiple sub-pathways of BER (short-path or longpatch) and newly designated DNA repair pathways (e.g., SSBR and NIR) that utilize BER proteins complicate any comprehensive understanding of BER and its role in genome maintenance, chemotherapeutic response, neurodegeneration, cancer or aging. Herein, we propose a unified model of BER, comprised of three functional processes: Lesion Recognition/Strand Scission, Gap Tailoring and DNA Synthesis/Ligation, each represented by one or more multiprotein complexes and coordinated via the XRCC1/DNA Ligase III and PARP1 scaffold proteins. …