Results 31 to 40 of about 17,972 (261)

Histone transfer among chaperones [PDF]

Biochemical Society Transactions, 2012
The eukaryotic processes of nucleosome assembly and disassembly govern chromatin dynamics, in which histones exchange in a highly regulated manner to promote genome accessibility for all DNA-dependent processes. This regulation is partly carried out by histone chaperones, which serve multifaceted roles in co-ordinating the interactions of histone ...
Wallace H, Liu, Mair E A, Churchill
openaire   +2 more sources

Chaperoning histones at the DNA repair dance

DNA Repair, 2021
Unlike all other biological molecules that are degraded and replaced if damaged, DNA must be repaired as chromosomes cannot be replaced. Indeed, DNA endures a wide variety of structural damage that need to be repaired accurately to maintain genomic stability and proper functioning of cells and to prevent mutation leading to disease.
Ujani Chakraborty, Zih-Jie Shen, Jessica Tyler   +2 more
openaire   +3 more sources

Molecular Size Analysis of Recombinant Importin-histone Complexes Using Analytical Ultracentrifugation

Bio-Protocol, 2020
Histones constitute the protein components of nucleosomes. Despite their small sizes, histones do not diffuse through the nuclear pore complex. Instead, they are transported to the nucleus by importins, either alone or in complex with histone chaperones.
Abhilash Padavannil, Chad Brautigam, Yuh Chook   +2 more
doaj   +1 more source

The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution [PDF]

, 2013
NAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a ...
El-Mkami, H., Bowman, A., Dmitri I. Svergun, Hammond, C. M., Hassane El-mkami, Ward, R., David G. Norman, Ward, Richard, Norman, David G., Owen-Hughes, Tom; id_orcid, Svergun, Dmitri, El-Mkami, Hassane, Richard Ward, Stirling, A., Svergun, Dmitri I., Owen-Hughes, Tom, Norman, D. G., Stirling, Andrew, Andrew Stirling, Bowman, Andrew, Shang, Weifeng, Robinson, David A., El Mkami, Hassane, Colin M. Hammond, Andrew Bowman, Hammond, Colin M., Shang, W., Robinson, D. A., David A. Robinson, Weifeng Shang, Tom Owen-hughes, Owen-Hughes, T.   +31 more
core   +1 more source

Catalytic activation of histone acetyltransferase Rtt109 by a histone chaperone [PDF]

Proceedings of the National Academy of Sciences, 2010
Most histone acetyltransferases (HATs) function as multisubunit complexes in which accessory proteins regulate substrate specificity and catalytic efficiency. Rtt109 is a particularly interesting example of a HAT whose specificity and catalytic activity require association with either of two histone chaperones, Vps75 or Asf1.
Kolonko, Erin M., Albaugh, Brittany N., Lindner, Scott E., Chen, Yuanyuan, Satyshur, Kenneth A., Arnold, Kevin M., Kaufman, Paul D., Keck, James G., Denu, John M.   +8 more
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The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation [PDF]

, 2011
Histone chaperones physically interact with histones to direct proper assembly and disassembly of nucleosomes regulating diverse nuclear processes such as DNA replication, promoter remodeling, transcription elongation, DNA damage, and histone variant ...
Bowman, Andrew, El Mkami, Hassane, Nicola Wiechens, Bowman, A., Vijender Singh, Andrew Bowman, David George Norman, Ward, Richard, Singh, Vijender, Owen-Hughes, Tom; id_orcid, El-Mkami, Hassane, Richard Ward, Hassane El-Mkami, Wiechens, Nicola, Norman, David George, Owen-Hughes, Tom, Tom Owen-Hughes   +16 more
core   +1 more source

Histone chaperone specificity in Rtt109 activation [PDF]

Nature Structural & Molecular Biology, 2008
Rtt109 is a histone acetyltransferase that requires a histone chaperone for the acetylation of histone 3 at lysine 56 (H3K56). Rtt109 forms a complex with the chaperone Vps75 in vivo and is implicated in DNA replication and repair. Here we show that both Rtt109 and Vps75 bind histones with high affinity, but only the complex is efficient for catalysis.
Young-Jun, Park, Keely B, Sudhoff, Andrew J, Andrews, Laurie A, Stargell, Karolin, Luger   +4 more
openaire   +2 more sources

Probing the (H3-H4)(2) histone tetramer structure using pulsed EPR spectroscopy combined with site-directed spin labelling [PDF]

, 2009
The (H3-H4)(2) histone tetramer forms the central core of nucleosomes and, as such, plays a prominent role in assembly, disassembly and positioning of nucleosomes.
Ward, Richard, Owen-Hughes, Tom; id_orcid, Norman, David G., Bowman, Andrew, El-Mkami, Hassane, Bowman, A., Owen-Hughes, Tom   +6 more
core   +1 more source

Histone chaperone ASF1 mediates H3.3-H4 deposition in Arabidopsis

Nature Communications, 2022
Histone chaperones and chromatin remodelers control nucleosome dynamics. Here the authors show that the Arabidopsis ASF1 chaperone primarily supplies histone variants to the HIRA complex to ensure proper epigenetic gene regulation.
Zhenhui Zhong, Yafei Wang, Ming Wang, Fan Yang, Quentin Angelo Thomas, Yan Xue, Yaxin Zhang, Wanlu Liu, Yasaman Jami-Alahmadi, Linhao Xu, Suhua Feng, Sebastian Marquardt, James A. Wohlschlegel, Israel Ausin, Steven E. Jacobsen   +14 more
doaj   +1 more source

Histone Chaperones and Digestive Cancer: A Comprehensive Review

, 2022
Histone chaperones are responsible for histone metabolism. Recent investigations have revealed that the abnormal expression of several histone chaperones in digestive cancer is associated with pathogenesis of digestive cancer.
Tianxiang Jiang, Zhaolun Cai, Bo Zhang, Zhou Zhao, Junhong Han   +4 more
core   +1 more source