scholarly journals The p53-regulated Cyclin-dependent Kinase Inhibitor, p21 (cip1, waf1, sdi1), Is Not Required for Global Genomic and Transcription-coupled Nucleotide Excision Repair of UV-induced DNA Photoproducts

2001 ◽  
Vol 276 (28) ◽  
pp. 25813-25822 ◽  
Author(s):  
Shanthi Adimoolam ◽  
Cindy X. Lin ◽  
James M. Ford
Keyword(s):  
Nucleotide Excision Repair ◽  
Kinase Inhibitor ◽  
Excision Repair ◽  
Cyclin Dependent Kinase ◽  
Cyclin Dependent Kinase Inhibitor ◽  
Nucleotide Excision ◽  
Dna Photoproducts

scholarly journals Inhibition of Nucleotide Excision Repair by the Cyclin-dependent Kinase Inhibitor p21

1995 ◽  
Vol 270 (37) ◽  
pp. 22008-22016 ◽  
Author(s):  
Zhen-Qiang Pan ◽  
Joyce T. Reardon ◽  
Lei Li ◽  
Hernan Flores-Rozas ◽  
Randy Legerski ◽  
...  
Keyword(s):  
Nucleotide Excision Repair ◽  
Kinase Inhibitor ◽  
Excision Repair ◽  
Cyclin Dependent Kinase ◽  
Cyclin Dependent Kinase Inhibitor ◽  
Nucleotide Excision

scholarly journals Nucleotide excision repair of DNA with recombinant human proteins: definition of the minimal set of factors, active forms of TFIIH, and modulation by CAK

2000 ◽  
Vol 14 (3) ◽  
pp. 349-359 ◽  
Author(s):  
Sofia J. Araújo ◽  
Franck Tirode ◽  
Frederic Coin ◽  
Helmut Pospiech ◽  
Juhani E. Syväoja ◽  
...  
Keyword(s):  
Nucleotide Excision Repair ◽  
Transcription Initiation ◽  
Kinase Inhibitor ◽  
Excision Repair ◽  
Muscular Atrophy ◽  
Minimal Set ◽  
Repair Synthesis ◽  
Dna Lesion ◽  
Nucleotide Excision ◽  
Recombinant Polypeptides

During human nucleotide excision repair, damage is recognized, two incisions are made flanking a DNA lesion, and residues are replaced by repair synthesis. A set of proteins required for repair of most lesions is RPA, XPA, TFIIH, XPC–hHR23B, XPG, and ERCC1–XPF, but additional components have not been excluded. The most complex and difficult to analyze factor is TFIIH, which has a 6-subunit core (XPB, XPD, p44, p34, p52, p62) and a 3-subunit kinase (CAK). TFIIH has roles both in basal transcription initiation and in DNA repair, and several inherited human disorders are associated with mutations in TFIIH subunits. To identify the forms of TFIIH that can function in repair, recombinant XPA, RPA, XPC–hHR23B, XPG, and ERCC1–XPF were combined with TFIIH fractions purified from HeLa cells. Repair activity coeluted with the peak of TFIIH and with transcription activity. TFIIH from cells with XPB or XPD mutations was defective in supporting repair, whereas TFIIH from spinal muscular atrophy cells with a deletion of one p44 gene was active. Recombinant TFIIH also functioned in repair, both a 6- and a 9-subunit form containing CAK. The CAK kinase inhibitor H-8 improved repair efficiency, indicating that CAK can negatively regulate NER by phosphorylation. The 15 recombinant polypeptides define the minimal set of proteins required for dual incision of DNA containing a cisplatin adduct. Complete repair was achieved by including highly purified human DNA polymerase δ or ε, PCNA, RFC, and DNA ligase I in reaction mixtures, reconstituting adduct repair for the first time with recombinant incision factors and human replication proteins.

p210 BCR/ABL kinase regulates nucleotide excision repair (NER) and resistance to UV radiation

Blood ◽  
2003 ◽  
Vol 102 (7) ◽  
pp. 2632-2637 ◽  
Author(s):  
Yvan Canitrot ◽  
Rafal Falinski ◽  
Thierry Louat ◽  
Guy Laurent ◽  
Christophe Cazaux ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Nucleotide Excision Repair ◽  
Kinase Inhibitor ◽  
Excision Repair ◽  
Ectopic Expression ◽  
Myeloid Cells ◽  
Lymphoid Cells ◽  
Nuclear Antigen ◽  
Abl Tyrosine Kinase ◽  
Nucleotide Excision

Abstract Both clinical and experimental evidence illustrate that p190 and p210 BCR/ABL oncogenic tyrosine kinases induce resistance to DNA damage and confer an intrinsic genetic instability. Here, we investigated whether BCR/ABL expression could modulate nucleotide excision repair (NER). We found that ectopic expression of p210 BCR/ABL in murine lymphoid BaF3 cell line inhibited NER activity in vitro, promoting hypersensitivity of these cells to ultraviolet (UV) treatment and facilitating a mutator phenotype. However, expression of p210 BCR/ABL in human and murine myeloid cell lines and primary bone marrow cells resulted in the increased NER activity and resistance to UV irradiation. The ABL tyrosine kinase inhibitor STI571 reversed these effects, showing that p210 BCR/ABL tyrosine kinase activity is responsible for deregulation of NER. Hypoactivity of NER in p210 BCR/ABL-positive lymphoid cells was accompanied by the decreased interaction between proliferating cell nuclear antigen (PCNA) and xeroderma pigmentosum group B (XPB); conversely, this interaction was enhanced in p210 BCR/ABL-positive myeloid cells. p190 BCR/ABL did not affect NER in lymphoid and myeloid cells. In summary, our study suggests that p210 BCR/ABL reduced NER activity in lymphoid cells, leading to hypersensitivity to UV and mutagenesis. In contrast, p210 BCR/ABL expression in myeloid cells facilitated NER and induced resistance to UV. (Blood. 2003;102:2632-2637)

MITF controls the interface of nucleotide excision repair and transcription through direct regulation of GTF2H1

2015 ◽  
Vol 227 (03) ◽  
Author(s):  
M Seoane ◽  
J Strauss ◽  
AC Puller ◽  
M Noshiravani ◽  
S Feldhaus ◽  
...  
Keyword(s):  
Nucleotide Excision Repair ◽  
Excision Repair ◽  
Nucleotide Excision ◽  
Direct Regulation
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