thông tin biểu ghi
  • Bài trích
  • Ký hiệu PL/XG: 664.022
    Nhan đề: Purification of Saccharomyces cerevisiae recombinant Crp1 /

DDC 664.022
Tác giả CN Phung, Thi Thu Huong
Nhan đề Purification of Saccharomyces cerevisiae recombinant Crp1 / Phung Thi Thu Huong, Tran Hong Diem
Thông tin xuất bản Tp. Hồ Chí Minh : Đại học Nguyễn Tất Thành, 2020
Mô tả vật lý 5 tr.
Tóm tắt A 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.
Từ khóa tự do Purification
Từ khóa tự do Crpl
Từ khóa tự do DNA binding
Từ khóa tự do Mus81
Nguồn trích Tạp chí Khoa học và Công nghệ - Đại học Nguyễn Tất Thành 2018tr. 22-26 Số: 04
000 00000nab#a2200000ui#4500
00128816
0029
004978A461D-5F06-426D-840A-29B501601584
005202106090921
008081223s2020 vm| vie
0091 0
039|y20210609092123|zngantk
082 |a664.022
100 |aPhung, Thi Thu Huong
245 |aPurification of Saccharomyces cerevisiae recombinant Crp1 / |cPhung Thi Thu Huong, Tran Hong Diem
260 |aTp. Hồ Chí Minh : |bĐại học Nguyễn Tất Thành, |c2020
300 |a5 tr.
520 |aA 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.
653 |aPurification
653 |aCrpl
653 |aDNA binding
653 |aMus81
690 |aViện Kỹ thuật Công nghệ cao NTT
773 |tTạp chí Khoa học và Công nghệ - Đại học Nguyễn Tất Thành |d2018|gtr. 22-26|x2615-9015|i04
890|a0|b0|c1|d38
Không tìm thấy biểu ghi nào