Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Birgitte Ø. Wittschieben"'
Publikováno v:
Cell Research. 18:174-183
Most current knowledge about DNA polymerase zeta (pol zeta) comes from studies of the enzyme in the budding yeast Saccharomyces cerevisiae, where pol zeta consists of a complex of the catalytic subunit Rev3 with Rev7, which associates with Rev1. Most
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae9347665d37b1c09ff54fc9704afc63
https://doi.org/10.1038/cr.2007.117
https://doi.org/10.1038/cr.2007.117
Publikováno v:
DNA Repair. 2:1065-1069
A group of recent publications contribute new insights concerning the role of the DNA damage-binding protein complex (DDB) in DNA repair. Mutations in the 48kDa DDB2 subunit are now found in all confirmed cases of xeroderma pigmentosum complementatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1ee0cb760bdbb04d6a75bfde9cd9962
https://doi.org/10.1016/s1568-7864(03)00113-7
https://doi.org/10.1016/s1568-7864(03)00113-7
Autor:
Jane Fellows, Paul Tempst, Birgitte Ø. Wittschieben, Reiko Ohba, Yang Li, C. David Allis, Gabriel Otero, Hediye Erdjument-Bromage, Jesper Q. Svejstrup, Therese de Bizemont
Publikováno v:
Molecular Cell. 4:123-128
The elongator complex is a major component of the RNA polymerase II (RNAPII) holoenzyme responsible for transcriptional elongation in yeast. Here we identify Elp3, the 60-kilodalton subunit of elongator/RNAPII holoenzyme, as a highly conserved histon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23f64dc1fe0d857ec93b1869d44c96a2
https://doi.org/10.1016/s1097-2765(00)80194-x
https://doi.org/10.1016/s1097-2765(00)80194-x
Publikováno v:
The Journal of biological chemistry. 280(48)
The DDB protein complex, comprising the subunits DDB1 and DDB2, binds tightly to UV light-irradiated DNA. Mutations in DDB2 are responsible for xeroderma pigmentosum group E, a disorder with defects in nucleotide excision repair of DNA. Both subunits
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd5073f01374a6f41b5ba1323426b3f7
https://pubmed.ncbi.nlm.nih.gov/16223728
https://pubmed.ncbi.nlm.nih.gov/16223728
Publikováno v:
The Journal of biological chemistry. 279(31)
The molecular architecture of six-subunit yeast holo-Elongator complex was investigated by the use of immunoprecipitation, two-hybrid interaction mapping, and in vitro studies of binary interactions between individual subunits. Surprisingly, Elp2 is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69ad98fbd98aab5ce134c2fa9ac821ed
https://pubmed.ncbi.nlm.nih.gov/15138274
https://pubmed.ncbi.nlm.nih.gov/15138274
Autor:
Bradley R. Cairns, Douglas N. Roberts, Jane L. Walker, Jesper Q. Svejstrup, Birgitte Ø. Wittschieben, Arnold Kristjuhan
Heterochromatin formation in yeast involves deacetylation of histones, but the precise relationship between acetylation and the association of proteins such as Sir3, Sir4, and the histone deacetylase Sir2 with chromatin is still unclear. Here we show
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e79dc6a9cd7ef0f95d0cb2c29b70c4db
https://europepmc.org/articles/PMC164624/
https://europepmc.org/articles/PMC164624/
Publikováno v:
Gene. 267(1)
Yeast cells lacking transcription elongation factor genes such as PPR2 (TFIIS) and ELP (Elongator) are viable and show deleterious phenotypes only when transcription is rendered less effective by RNA polymerase mutations or by decreasing nucleotide p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f1fdbfc4e9855fc43b44b26476f9900
https://pubmed.ncbi.nlm.nih.gov/11311553
https://pubmed.ncbi.nlm.nih.gov/11311553
Elp3 and Gcn5 are histone acetyltransferases (HATs) that function in transcription as subunits of Elongator and SAGA/ADA, respectively. Here we show that mutations that impair the in vitro HAT activity of Elp3 confer typical elp phenotypes such as te
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b21f069e8ac4f32c47077756355d7c44
https://europepmc.org/articles/PMC203375/
https://europepmc.org/articles/PMC203375/
Publikováno v:
Biochemical Society Transactions. 28:A62-A62
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::90f23481963cf52b08491bb7d7be9729
https://doi.org/10.1042/bst028a062b
https://doi.org/10.1042/bst028a062b