Results 51 to 60 of about 31,898 (266)

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

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
openaire   +3 more sources

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

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

Histone modifications and the HtrA-like serine protease Nma111p regulate apoptosis in budding yeast [PDF]

, 2010
Histone modifications and the HtrA-like serine protease Nma111p regulate apoptosis in budding yeast David Walter, 2010, PhD Thesis, University of Basel Apoptosis is a form of programmed cell death that plays a central role in development and ...
Walter, David
core   +1 more source

Histone Chaperones as Cardinal Players in Development

Frontiers in Cell and Developmental Biology, 2022
Dynamicity and flexibility of the chromatin landscape are critical for most of the DNA-dependent processes to occur. This higher-order packaging of the eukaryotic genome into the chromatin is mediated by histones and associated non-histone proteins that determine the states of chromatin.
Sruthy Manuraj Rajam, Sruthy Manuraj Rajam, Pallavi Chinnu Varghese, Pallavi Chinnu Varghese, Debasree Dutta   +4 more
openaire   +3 more sources

Acetylation of histone H3 at lysine 64 regulates nucleosome dynamics and facilitates transcription [PDF]

, 2014
Post-translational modifications of proteins have emerged as a major mechanism for regulating gene expression. However, our understanding of how histone modifications directly affect chromatin function remains limited.
Holzner, M. (M), Eleni Kallis, Holzner, M., Michaelis, J., Richter, F. (F) M. (M), Ryan, D. (D) P. (P), Feldmann, A. (A), Daniel P Ryan, Owen-Hughes, Tom; id_orcid, Kacem, S., Tropberger, Philipp, Di Cerbo, V., Bannister, A., Kallis, E. (E), Michaelis, Jens, Feldmann, A., Richter, Florian, Martin, Daujat, S. (Sylvain), Robert Schneider, Richter, F., Tropberger, P., Hoerner, Leslie, Richter, Florian Martin, Mittler, G. (G), Emilie Montellier, Di Cerbo, V. (V), Feil, Robert, Bannister, A. (A) J. (J), Vincenzo Di Cerbo, Ryan, D., Kallis, Eleni, Ryan, D. P., Di Cerbo, Vincenzo, Owen-Hughes, T. (T), Leslie Hoerner, Jens Michaelis, Kallis, E., Khochbin, S. (S), Saadi Khochbin, Schneider, Robert, Holzner, Monika, Monika Holzner, Feil, R. (R), Ryan, Daniel, P., Feldmann, Angelika, Tom Owen-Hughes, Owen-Hughes, T., Bannister, A. J., Feil, R., Mohn, F., Hoerner, L., Fabio Mohn, Richter, F. M., Montellier, E. (E), Mittler, G., Schuebeler, D., Montellier, Emilie, Mohn, F. (F), Tropberger, P. (P), Angelika Feldmann, Owen-Hughes, Tom, Kacem, Salim, Mittler, Gerhard, Daujat, Sylvain, Montellier, E., Schneider, R., Dirk Schuebeler, Schuebeler, D. (D), Bannister, Andrew J., Hoerner, L. (L), Khochbin, S., Schneider, R. (Robert), Schuebeler, Dirk, Salim Kacem, Philipp Tropberger, Mohn, Fabio, Florian Martin Richter, Kacem, S. (S), Sylvain Daujat, Ryan, Daniel P., Andrew J Bannister, Khochbin, Saadi, Gerhard Mittler, Michaelis, J. (J), Robert Feil, Daujat, S.   +85 more
core   +1 more source

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 Variants and Their Chaperones in Hematological Malignancies

HemaSphere, 2023
Epigenetic regulation occurs on the level of compacting DNA into chromatin. The functional unit of chromatin is the nucleosome, which consists of DNA wrapped around a core of histone proteins. While canonical histone proteins are incorporated into chromatin through a replication-coupled process, structural variants of histones, commonly named histone ...
Kirkiz, Ecem, Buschbeck, Marcus, Grebien, Florian, Meers, Oliver   +3 more
openaire   +3 more sources

Mitochondrial stress in advanced fibrosis and cirrhosis associated with chronic hepatitis B, chronic hepatitis C, or nonalcoholic steatohepatitis

Hepatology, EarlyView., 2022
Adaptive mitochondrial mechanisms allow mitochondrial resilience and prevent the worsening of fibrosis, while deregulation of these mechanisms promotes the progression from no/minimal‐mild (F0‐F2) fibrosis to advanced fibrosis and cirrhosis (F3‐F4). Abstract Background and Aims Hepatitis B virus (HBV) infection causes oxidative stress (OS) and alters ...
Dimitri Loureiro, Issam Tout, Stéphanie Narguet, Cheikh Mohamed Bed, Morgane Roinard, Ahmad Sleiman, Nathalie Boyer, Nathalie Pons‐Kerjean, Corinne Castelnau, Nathalie Giuly, Dorothy Tonui, Vassili Soumelis, Jamel El Benna, Patrick Soussan, Richard Moreau, Valérie Paradis, Abdellah Mansouri, Tarik Asselah   +17 more
wiley   +1 more source