Detailed Information

Cited 0 time in webofscience Cited 0 time in scopus
Metadata Downloads

The DNA repair domain of human rpS3 protects against photoaging by removing cyclobutane pyrimidine dimers

Authors
Yang, Hee WoongKim, Hag DongKim, Joon
Issue Date
8월-2019
Publisher
WILEY
Keywords
Cell-penetrating peptides; cyclobutane pyrimidine dimers; DNA repair; matrix metalloproteinase-1; ribosomal protein S3; UV irradiation
Citation
FEBS LETTERS, v.593, no.15, pp.2060 - 2068
Indexed
SCIE
SCOPUS
Journal Title
FEBS LETTERS
Volume
593
Number
15
Start Page
2060
End Page
2068
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/63682
DOI
10.1002/1873-3468.13479
ISSN
0014-5793
Abstract
Ribosomal protein S3 (rpS3) has endonuclease activity for DNA repair. In particular, rpS3 cleaves the phosphodiester bonds of damaged DNA. In this study, we show that the repair domain of rpS3 spans amino acids 144-189. We fused rpS3 with the transactivator of transcription (TAT) sequence to introduce the rpS3 repair domain into cells. We find that the TAT-rpS3 (aa: 144-189) peptide cleaves UV-induced cyclobutane pyrimidine dimers (CPDs) in cells. We also reveal that the TAT-rpS3 peptide reduces matrix metalloproteinase-1 (MMP-1) induction in UV-irradiated fibroblasts and increases cell migration activity. Taken together, our study suggests that penetration of the rpS3 repair domain into cells can cleave UV-induced CPDs and reduce MMP-1 expression induced by UV.
Files in This Item
There are no files associated with this item.
Appears in
Collections
Graduate School > Department of Life Sciences > 1. Journal Articles

qrcode

Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.

Altmetrics

Total Views & Downloads

BROWSE