A newly identified photolyase from Arthrospira platensis possesses a unique methenyltetrahydrofolate chromophore-binding pattern

FEBS Lett. 2020 Feb;594(4):740-750. doi: 10.1002/1873-3468.13657. Epub 2019 Nov 24.

Abstract

Cyclobutane pyrimidine dimers (CPD), as a common DNA damage caused by UV radiation, often lead to skin cancer. Here, we identified a photolyase from the alga Arthrospira platensis (designated as Ap-phr), which has been regarded as a safe organism for humans for centuries, that can efficiently repair CPD lesions in ssDNA and dsDNA in vitro. The 1.6 Å resolution crystal structure of Ap-phr revealed that it possesses a unique methenyltetrahydrofolate chromophore-binding pattern with high energy transfer efficiency. Our study of Ap-phr highlights its potential use in cosmetic, industrial and aesthetic medicine applications.

Keywords: Ap-phr; CRY-DASH; MTHF; crystal structure; enzyme activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • DNA, Single-Stranded / metabolism
  • Deoxyribodipyrimidine Photo-Lyase / chemistry
  • Deoxyribodipyrimidine Photo-Lyase / metabolism*
  • Models, Molecular
  • Phylogeny
  • Protein Conformation
  • Spirulina / enzymology*
  • Tetrahydrofolates / metabolism*

Substances

  • DNA, Single-Stranded
  • Tetrahydrofolates
  • 5,10-methenyltetrahydrofolate
  • Deoxyribodipyrimidine Photo-Lyase

Supplementary concepts

  • Arthrospira platensis