Evidence map›Paper›PMID 33464383›Full record

ArticleCellular and molecular life sciences : CMLS2021

Ribosomal protein S3 associates with the TFIIH complex and positively regulates nucleotide excision repair.

Y J Park, S H Kim, T S Kim, S M Lee, B S Cho, C I Seo, H D Kim, J Kim

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.1field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Chromatin topology control by a muscle-specific ribosomal protein.bioRxiv : the preprint server for biology · 2026
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  11. Cells · 2023
    Article
  12. Review
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  14. Review
  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Y J ParkLab of Biochemistry, Division of Life Sciences, Korea University, Seoul, 02841, Korea.
S H KimLab of Biochemistry, Division of Life Sciences, Korea University, Seoul, 02841, Korea.
T S KimLab of Biochemistry, Division of Life Sciences, Korea University, Seoul, 02841, Korea.
S M LeeLab of Biochemistry, Division of Life Sciences, Korea University, Seoul, 02841, Korea.
B S ChoLab of Biochemistry, Division of Life Sciences, Korea University, Seoul, 02841, Korea.
C I SeoLab of Biochemistry, Division of Life Sciences, Korea University, Seoul, 02841, Korea.
H D KimTechnoComplex Building, HAEL Lab, Korea University, Seoul, 02841, Korea.
J KimLab of Biochemistry, Division of Life Sciences, Korea University, Seoul, 02841, Korea. joonkim@korea.ac.kr.ORCID http://orcid.org/0000-0003-0914-4273
Korea University · KR

Funding

National Research Foundation of Korea NRF-2019S1A5A2A03050121National Research Foundation of Korea NRF-2020R1A2C2100803
6 · The paper itself

Abstract

In mammalian cells, the bulky DNA adducts caused by ultraviolet radiation are mainly repaired via the nucleotide excision repair (NER) pathway; some defects in this pathway lead to a genetic disorder known as xeroderma pigmentosum (XP). Ribosomal protein S3 (rpS3), a constituent of the 40S ribosomal subunit, is a multi-functional protein with various extra-ribosomal functions, including a role in the cellular stress response and DNA repair-related activities. We report that rpS3 associates with transcription factor IIH (TFIIH) via an interaction with the xeroderma pigmentosum complementation group D (XPD) protein and complements its function in the NER pathway. For optimal repair of UV-induced duplex DNA lesions, the strong helicase activity of the TFIIH complex is required for unwinding damaged DNA around the lesion. Here, we show that XP-D cells overexpressing rpS3 showed markedly increased resistance to UV radiation through XPD and rpS3 interaction. Additionally, the knockdown of rpS3 caused reduced NER efficiency in HeLa cells and the overexpression of rpS3 partially restored helicase activity of the TFIIH complex of XP-D cells in vitro. We also present data suggesting that rpS3 is involved in post-excision processing in NER, assisting TFIIH in expediting the repair process by increasing its turnover rate when DNA is damaged. We propose that rpS3 is an accessory protein of the NER pathway and its recruitment to the repair machinery augments repair efficiency upon UV damage by enhancing XPD helicase function and increasing its turnover rate.

Indexed as

DNA DamageDNA RepairDNA AdductsDNA HelicasesHeLa CellsHumansRibosomal ProteinsTranscription Factor TFIIHXeroderma PigmentosumXeroderma Pigmentosum Group D ProteinDNA AdductsDNA HelicasesERCC2 protein, humanRibosomal Proteinsribosomal protein S3Transcription Factor TFIIHXeroderma Pigmentosum Group D ProteinExtra-ribosomal functionNERrpS3TFIIHXPD

Identifiers

PMID33464383
PMCPMC11072392
OpenAlexW3125890444

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.