Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 3 of 3
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 …
Fanconi Anemia Protein Fancd2 Inhibits Trf1 Polyadp-Ribosylation Through Tankyrase1-Dependent Manner, Alex Lyakhovich, Maria Ramirez, Andres Castella, Amanda Simons, Jeffrey Parvin, Jordi Suralles
Fanconi Anemia Protein Fancd2 Inhibits Trf1 Polyadp-Ribosylation Through Tankyrase1-Dependent Manner, Alex Lyakhovich, Maria Ramirez, Andres Castella, Amanda Simons, Jeffrey Parvin, Jordi Suralles
Amanda Simons
Background: Fanconi anemia (FA) is a rare autosomal recessive syndrome characterized by developmental abnormalities, progressive bone marrow failure, and predisposition to cancer. The key FA protein FANCD2 crosstalks with members of DNA damage and repair pathways that also play a role at telomeres. Therefore, we investigated whether FANCD2 has a similar involvement at telomeres. Results: We reveal that FANCD2 may perform a novel function separate to the FANCD2/BRCA pathway. This function includes FANCD2 interaction with one of the telomere components, the PARP family member tankyrase-1. Moreover, FANCD2 inhibits tankyrase-1 activity in vitro. In turn, FANCD2 deficiency increases the polyADPribosylation of …