Structural insights into the duplex DNA processing of TREX2

Author:

Cheng Hiu-Lo1,Lin Chun-Ting2,Huang Kuan-Wei2,Wang Shuying34,Lin Yeh-Tung2,Toh Shu-Ing25,Hsiao Yu-Yuan125ORCID

Affiliation:

1. Institute of Bioinformatics and Systems Biology, National Chiao Tung University, Hsinchu, Taiwan 30050, ROC

2. Department of Biological Science and Technology, National Chiao Tung University, Hsinchu, Taiwan 30068, ROC

3. Department of Microbiology and Immunology, College of Medicine, National Cheng Kung University, Tainan, Taiwan 70101, ROC

4. Center of Infectious Disease and Signaling Research, National Cheng Kung University, Tainan, Taiwan 70101, ROC

5. Institute of Molecular Medicine and Bioengineering, National Chiao Tung University, Hsinchu, Taiwan 30068, ROC

Funder

Ministry of Science and Technology, Taiwan

Publisher

Oxford University Press (OUP)

Subject

Genetics

Reference54 articles.

1. A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein;Hoss;EMBO J.,1999

2. Identification and expression of the TREX1 and TREX2 cDNA sequences encoding mammalian 3′→5′ exonucleases;Mazur;J. Biol. Chem.,1999

3. DNA binding induces active site conformational change in the human TREX2 3′-exonuclease;de Silva;Nucleic Acids Res.,2009

4. The human TREX2 3′ → 5′-exonuclease structure suggests a mechanism for efficient nonprocessive DNA catalysis;Perrino;J. Biol. Chem.,2005

5. Biochemical and cellular characteristics of the 3′ → 5′ exonuclease TREX2;Chen;Nucleic Acids Res.,2007

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