Replication-related genes are upregulated in XP-A cells after UV-C irradiation.

Background: Xeroderma pigmentosum (XP) is hereditary disorder characterized by photosensitivity, predisposition to skin cancers of sun-exposed body sites and progressive neurologic symptoms in some cases. Cells from XP patients show higher sensitivity to ultraviolet radiation (UV) than normal cells.

Objective: We aimed to ascertain the genes differentially regulated in XP complementation group A (XP-A) cells after UV irradiation.

Mitotic genes are transcriptionally upregulated in the fibroblast irradiated with very low doses of UV-C.

Ultraviolet (UV) radiation induces a variety of biological effects, including DNA damage response and cell signaling pathways. We performed transcriptome analysis using microarray in human primary cultured fibroblasts irradiated with UV-C (0.5 or 5 J/m(2)) and harvested at 4 or 12 h following UV exposure.

Salicylic acid resistance is conferred by a novel YRR1 mutation in Saccharomyces cerevisiae.

Yeast cells can extrude intracellular drugs through membrane-associated efflux pumps, such as ATP-binding cassette (ABC) transporters and members of the major facilitator superfamily. Gene expression of drug efflux pumps is regulated by several transcription factors involved in pleiotropic drug resistance (PDR). Salicylic acid (SA) possesses weak antifungal activity.

Inhibition of nucleotide excision repair by anti-XPA monoclonal antibodies which interfere with binding to RPA, ERCC1, and TFIIH.

The xeroderma pigmentosum group A protein (XPA) binds to three nucleotide excision repair (NER) factors: RPA, ERCC1, and TFIIH. XPA also binds preferentially to UV- or chemical carcinogen-damaged DNA. In this study, we prepared anti-XPA monoclonal antibodies and examined their effects on NER.

The base substitution fidelity of DNA polymerase beta-dependent single nucleotide base excision repair.

Damaged DNA bases are removed from mammalian genomes by base excision repair (BER). Single nucleotide BER requires several enzymatic activities, including DNA polymerase and 5',2'-deoxyribose-5-phosphate lyase. Both activities are intrinsic to four human DNA polymerases whose base substitution error rate during gap-filling DNA synthesis varies by more than 10,000-fold.