Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Clayton B. Woodcock"'
Autor:
John R. Horton, Clayton B. Woodcock, Sifa B. Opot, Norbert O. Reich, Xing Zhang, Xiaodong Cheng
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-9 (2019)
CcrM is a cell cycle-regulated DNA methyltransferase that methylates an adenine within a specific sequence following replication in the gram negative bacterium Caulobacter crescentus. Here the authors present a crystal structure of DNA-bound CcrM tha
Externí odkaz:
https://doaj.org/article/4b19d54306f64a6a987f9f163c1d7c87
Autor:
Shaobo Dai, John R. Horton, Clayton B. Woodcock, Alex W. Wilkinson, Xing Zhang, Or Gozani, Xiaodong Cheng
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-8 (2019)
SETD3 is the first known metazoan protein histidine methyltransferase but the molecular basis for its target specificity is unclear. Here, the authors elucidate the structural and molecular determinants for the histidine specificity of SETD3.
Externí odkaz:
https://doaj.org/article/f2129526184a4597af28ea92c757a4b4
Biochemical and structural basis for YTH domain of human YTHDC1 binding to methylated adenine in DNA
Autor:
Clayton B. Woodcock, Robert Blumenthal, John R. Horton, Jujun Zhou, Mark T. Bedford, Xing Zhang, Xiaodong Cheng
Publikováno v:
Nucleic Acids Research
The recently characterized mammalian writer (methyltransferase) and eraser (demethylase) of the DNA N6-methyladenine (N6mA) methyl mark act on single-stranded (ss) and transiently-unpaired DNA. As YTH domain-containing proteins bind N6mA-containing R
Publikováno v:
Nucleic Acids Research
S-adenosyl-l-methionine dependent methyltransferases catalyze methyl transfers onto a wide variety of target molecules, including DNA and RNA. We discuss a family of methyltransferases, those that act on the amino groups of adenine or cytosine in DNA
Autor:
Clayton B. Woodcock, Sifa B. Opot, Norbert O. Reich, John R. Horton, Xing Zhang, Xiaodong Cheng
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-9 (2019)
Nature Communications
Nature Communications
The Caulobacter crescentus cell cycle-regulated DNA methyltransferase (CcrM) methylates the adenine of hemimethylated GANTC after replication. Here we present the structure of CcrM in complex with double-stranded DNA containing the recognition sequen
Publikováno v:
The Journal of biological chemistry, vol 293, iss 49
Two DNA methyltransferases, Dam and β-class cell cycle-regulated DNA methyltransferase (CcrM), are key mediators of bacterial epigenetics. CcrM from the bacterium Caulobacter crescentus (CcrM C. crescentus, methylates adenine at 5'-GANTC-3') display
Autor:
Nicolas L. Young, Matthew V. Holt, Xiaodong Cheng, Clayton B. Woodcock, Shaobo Dai, Alex W. Wilkinson, Xing Zhang, Anamika Patel, John R. Horton
Publikováno v:
J Biol Chem
Most characterized protein methylation events encompass arginine and lysine N-methylation, and only a few cases of protein methionine thiomethylation have been reported. Newly discovered oncohistone mutations include lysine-to-methionine substitution
Autor:
Dan Yu, Clayton B. Woodcock, Ivan R. Corrêa, Yun Huang, Masoud Vedadi, Jia Li, Taraneh Hajian, Xiaodong Cheng, Xing Zhang, Nan Dai, Tao Wu
Publikováno v:
Cell Discovery
Cell Discovery, Vol 5, Iss 1, Pp 1-4 (2019)
Cell Discovery, Vol 5, Iss 1, Pp 1-4 (2019)
Publikováno v:
Biochemistry. 56:3913-3922
Caulobacter crescentus relies on DNA methylation by the cell cycle-regulated methyltransferase (CcrM) in addition to key transcription factors to control the cell cycle and direct cellular differentiation. CcrM is shown here to efficiently methylate
Publikováno v:
Cell Discovery
Cell Discovery, Vol 5, Iss 1, Pp 1-3 (2019)
Cell Discovery, Vol 5, Iss 1, Pp 1-3 (2019)