The mechanism of gap creation by a multifunctional nuclease during base excision repair-Reference-Cited by-同舟云学术

The mechanism of gap creation by a multifunctional nuclease during base excision repair

Author:

Yoo Jungmin¹²³^ORCID,Lee Donghun¹²³^ORCID,Im Hyeryeon¹²,Ji Sangmi¹²,Oh Sanghoon²⁴^ORCID,Shin Minsang⁵^ORCID,Park Daeho¹³^ORCID,Lee Gwangrog¹²³⁴^ORCID

Affiliation:

1. School of Life Sciences, Gwangju Institute of Science and Technology, Gwangju 61005, Korea.

2. Single-Molecule Biology Laboratory, Gwangju Institute of Science and Technology, Gwangju 61005, Korea.

3. Cell Mechanobiology Laboratory, Gwangju Institute of Science and Technology, Gwangju 61005, Korea.

4. Department of Biomedical Science and Engineering, Gwangju Institute of Science and Technology, Gwangju 61005, Korea.

5. Department of Microbiology, School of Medicine, Kyungpook National University, 680 Gukchaebosang-Ro, Jung-gu, Daegu 41944, Korea.

Abstract

ExoIII tightly anchors itself at the AP site, cuts the backbone, and processively digests the downstream DNA without dissociation.

Funder

National Research Foundation of Korea

Norsk Revmatikerforbund

Ministrstvo za zdravje

Ministry of Health and Welfare, Republic of Korea

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference50 articles.

4. XthA (Exonuclease III) regulates loading of RecA onto DNA substrates in log phase Escherichia coli cells;Centore R. C.;Mol. Microbiol.,2008

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