Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Brian R Chapados"'
Autor:
Samantha G Zeitlin, Brian R Chapados, Norman M Baker, Caroline Tai, Geir Slupphaug, Jean Y J Wang
Publikováno v:
PLoS ONE, Vol 6, Iss 3, p e17151 (2011)
Uracil is removed from DNA by the conserved enzyme uracil DNA N-glycosylase (UNG). Previously, we observed that inhibiting UNG in Xenopus egg extracts blocked assembly of CENP-A, a histone H3 variant. CENP-A is an essential protein in all species, si
Externí odkaz:
https://doaj.org/article/daa6d77585eb4b38b51f181627e19706
Publikováno v:
Biochemical Society Transactions. 38:433-437
FENs (flap endonucleases) and related FEN-like enzymes [EXO-1 (exonuclease-1), GEN-1 (gap endonuclease 1) and XPG (xeroderma pigmentosum complementation group G)] are a family of bivalent-metal-ion-dependent nucleases that catalyse structure-specific
Autor:
Brian R. Chapados, Samantha G. Zeitlin, Evi Soutoglou, Michael W. Berns, Norman M. Baker, Don W. Cleveland, Jean Y. J. Wang
Publikováno v:
Zeitlin, SG; Baker, NM; Chapados, BR; Soutoglou, E; Wang, JYJ; Berns, MW; et al.(2009). Double-strand DNA breaks recruit the centromeric histone CENP-A. Proceedings of the National Academy of Sciences of the United States of America, 106(37), 15762-15767. doi: 10.1073/pnas.0908233106. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/3z3776mp
The histone H3 variant CENP-A is required for epigenetic specification of centromere identity through a loading mechanism independent of DNA sequence. Using multiphoton absorption and DNA cleavage at unique sites by I- Sce I endonuclease, we demonstr
Autor:
Jane A. Grasby, John A. Tainer, Karl Syson, Nicholas H. Williams, Christopher G. Tomlinson, Brian R. Chapados, Jon R. Sayers
Publikováno v:
Journal of Biological Chemistry. 283:28741-28746
Protein nucleases and RNA enzymes depend on divalent metal ions to catalyze the rapid hydrolysis of phosphate diester linkages of nucleic acids during DNA replication, DNA repair, RNA processing, and RNA degradation. These enzymes are widely proposed
Autor:
John A. Tainer, Brian R. Chapados, Sangeetha Vijayakumar, Kristina H. Schmidt, Alan E. Tomkinson, Richard D. Kolodner
Publikováno v:
Nucleic Acids Research
There is compelling evidence that proliferating cell nuclear antigen (PCNA), a DNA sliding clamp, co-ordinates the processing and joining of Okazaki fragments during eukaryotic DNA replication. However, a detailed mechanistic understanding of functio
Publikováno v:
Nucleic Acids Research
Proliferating cell nuclear antigen (PCNA) acts as a biologically essential processivity factor that encircles DNA and provides binding sites for polymerase, flap endonuclease-1 (FEN-1) and ligase during DNA replication and repair. We have computation
Autor:
Brian R. Chapados, June Hyung Lee, Erik W. Debler, James R. Williamson, Anette Schneemann, Jeffrey A. Chao
Publikováno v:
Nature Structural & Molecular Biology. 12:952-957
As a counter-defense against antiviral RNA silencing during infection, the insect Flock House virus (FHV) expresses the silencing suppressor protein B2. Biochemical experiments show that B2 binds to double-stranded RNA (dsRNA) without regard to lengt
Autor:
John A. Tainer, David J. Hosfield, Biana Yelent, Binghui Shen, Seungil Han, Junzhuan Qiu, Brian R. Chapados
Publikováno v:
Cell. 116(1):39-50
Flap EndoNuclease-1 (FEN-1) and the processivity factor proliferating cell nuclear antigen (PCNA) are central to DNA replication and repair. To clarify the molecular basis of FEN-1 specificity and PCNA activation, we report here structures of FEN-1:D
Publikováno v:
Biochemical and Biophysical Research Communications. 286:1073-1081
RNA primer removal during DNA replication is dependent on ribonucleotide- and structure-specific RNase H and FEN-1 nuclease activities. A specific RNase H involved in this reaction has long been sought. RNase HII is the only open reading frame in Arc
Publikováno v:
The Journal of Organic Chemistry. 65:1210-1214