Difference between revisions of "Part:BBa K4765019"

 
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XRCC1 is a vital protein in DNA repair, particularly for single-strand breaks caused by radiation and alkylating agents.
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===Introduction===
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XRCC1 is a vital protein in DNA repair, particularly for single-strand breaks caused by radiation and alkylating agents. It collaborates with DNA ligase III, polymerase beta, and poly (ADP-ribose) polymerase in base excision repair. It might also play a role in meiosis-related DNA processes. Although XRCC1 lacks enzymatic activity, it acts as a scaffold for repair enzymes, aiding in single-strand break repair, base excision repair, and nucleotide excision repair<ref>London R. E. (2015). The structural basis of XRCC1-mediated DNA repair. DNA repair, 30, 90–103. https://doi.org/10.1016/j.dnarep.2015.02.005</ref>. XRCC1's structure includes three domains, enabling interactions with various repair proteins. Additionally, it is involved in error-prone microhomology-mediated end joining repair of double-strand breaks, often leading to mutation-inducing deletions.
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===Usage and Biology===
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We heterologously expressed codon-optimized XRCC1 in ''E. coli'', endowing it with anti-UV capability.
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===Characterization===
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==Reference==

Revision as of 08:01, 1 October 2023


XRCC1

Introduction

XRCC1 is a vital protein in DNA repair, particularly for single-strand breaks caused by radiation and alkylating agents. It collaborates with DNA ligase III, polymerase beta, and poly (ADP-ribose) polymerase in base excision repair. It might also play a role in meiosis-related DNA processes. Although XRCC1 lacks enzymatic activity, it acts as a scaffold for repair enzymes, aiding in single-strand break repair, base excision repair, and nucleotide excision repair[1]. XRCC1's structure includes three domains, enabling interactions with various repair proteins. Additionally, it is involved in error-prone microhomology-mediated end joining repair of double-strand breaks, often leading to mutation-inducing deletions.

Usage and Biology

We heterologously expressed codon-optimized XRCC1 in E. coli, endowing it with anti-UV capability.

Characterization

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 685
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 1735


Reference

  1. ↑ London R. E. (2015). The structural basis of XRCC1-mediated DNA repair. DNA repair, 30, 90–103. https://doi.org/10.1016/j.dnarep.2015.02.005