Purification of Saccharomyces cerevisiae recombinant Crp1

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dc.contributor.authorPhung, Thi Thu Huong
dc.contributor.authorTran, Hong Diem
dc.date.accessioned2024-08-23T07:25:54Z
dc.date.accessioned2024-08-29T02:18:22Z
dc.date.available2024-08-23T07:25:54Z
dc.date.available2024-08-29T02:18:22Z
dc.date.issued2018
dc.description5 pages.
dc.description.abstractA complex Mus81-Mm4 is a DNA structure–specific endonuclease in Saccharomyces cerevisiae. Mus81-Mms4 functions in processing of recombination intermediates that could arise during the repair of stalled and blocked replication forks and double stranded breaks. Mus81-Mms4 works with many proteins involved in DNA repair, replication fork stability, and joint molecule formation/resolution during homologous recombination repair. A biochemical screening of protein(s) that enhances the Mus81-Mms4 endonuclease activity on its preferable substrates in vitro revealed that Crp1, a cruciform DNA-recognizing protein, which can specifically bind to DNA four-way junction structures like Holliday junctions could be the potential factor. To further demonstrate that Crp1 interacts functionally with Mus81-Mms4 in vitro, we carried out the purification of recombinant Crp1 using Escherichia coli system. Our results showed that the purified Crp1 was highly homogenous and active that is ready for biochemical use.
dc.identifier.citationNguyen Tat Thanh University. (2018). Journal of Science and Technology - NTTU, Volume 1, No 04. ISSN 2615-9015.
dc.identifier.issn2615-9015
dc.identifier.urihttps://repository.ntt.edu.vn/handle/298300331/50295
dc.language.isoen
dc.publisherNguyen Tat Thanh University
dc.subjectCrp1
dc.subjectDNA binding
dc.subjectMus81
dc.subjectPurification
dc.titlePurification of Saccharomyces cerevisiae recombinant Crp1
dc.typeArticle

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