dict.md logo
Choose languages of interest
SELECT >>
English
Advertisement:
Translation
 
0 translations
 
Definition
 
enEnglish
histone binding definition: Interacting selectively with a histone, any of a group of water-soluble proteins found in association with the DNA of plant and animal chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in nonspecific suppression of gene activity. [GOC:jl]
histone acetyltransferase binding definition: Interacting selectively with the enzyme histone acetyltransferase. [GOC:bf]
histone deacetylase binding definition: Interacting selectively with the enzyme histone deacetylase. [GOC:jl]
methylated histone residue binding definition: Interacting selectively with a methylated residue on a histone protein. Histones are any of a group of water-soluble proteins found in association with the DNA of plant and animal chromosomes. [GOC:bf, PMID:14585615]
Histone Acetyltransferase MYST2 definition: The histone acetyltransferase MYST2 (611 aa, 71 kD) is encoded by the human MYST2 gene. This soluble, nuclear protein may play a role in transcription by RNA polymerase II.
MYST2 Gene definition: This gene is involved in epigenetic control of gene expression.
nucleosomal histone binding definition: Interacting selectively with a histone that is assembled into a nucleosome. [GOC:mah]
MYST2 wt Allele definition: Human MYST2 wt allele is located in the vicinity of 17q21.32 and is approximately 40 kb in length. This allele, which encodes histone acetyltransferase MYST2 protein, may play a role in activation and repression of RNA polymerase II transcription.
 
Publications
 

Regulation of chromatin binding by a conformational switch in the tail of the Ran exchange factor RCC1: ... with DNA but inhibits histone binding. Apo-Ran significantly ...

Yi Hao et al.

The Journal of Cell Biology , 08 Sep 2008

Analysis of Groucho–histone interactions suggests mechanistic similarities between Groucho- and Tup1-mediated repression: ... Our analysis of Gro–histone interactions provides further support for a close evolutionary relationship between Gro and Tup1. In particular, we show that, as with the N-terminal region of Tup1, the N-terminal region of Gro is necessary and sufficient for direct binding to histones. The ...

Rubén D. Flores-Saaib et al.

Nucleic Acids Research , 01 Nov 2000

A Thermodynamic Model for Nap1-Histone Interactions *: ... by facilitating histone exchange as well as nucleosome assembly and disassembly. It has been suggested that yNap1 carries out these functions by regulating the concentration of free histones. Therefore, a quantitative understanding of yNap1-histone interactions also provides information on the thermodynamics of chromatin. We have developed quantitative methods to study the affinity of yNap1 for histones. We show that yNap1 binds H2A/H2B and H3/H4 histone complexes with low n m affinity, and that each yNap1 dimer binds two histone fold dimers. The yNap1 tails contribute synergistically to histone binding while the histone tails ...

Andrew J. Andrews et al.

The Journal of Biological Chemistry , 21 Nov 2008

A NASP (N1/N2)-Related Protein, Sim3, Binds CENP-A and Is Required for Its Deposition at Fission Yeast Centromeres: ... is the presence of the histone H3 variant CENP-A Cnp1 . It is not known how CENP-A Cnp1 is specifically delivered to, and assembled into, centromeric chromatin. Through a screen for factors involved in kinetochore integrity in fission yeast, we identified Sim3. Sim3 is homologous to known histone binding proteins NASP Human ...

Elaine M. Dunleavy et al.

Molecular Cell , 28 Dec 2007

Histones bind more tightly to bromodeoxyuridine-substituted DNA than to normal DNA.: ... DNA with respect to histone binding. The tighter binding of ...

S Lin et al.

Nucleic Acids Research , 01 Sep 1976

The detection of DNA-binding proteins by protein blotting.: ... RNA-binding proteins or histone-binding proteins by incubation ...

B Bowen et al.

Nucleic Acids Research , 11 Jan 1980

The transcriptional cofactor MIER1-beta negatively regulates histone acetyltransferase activity of the CREB-binding protein

Tina M Blackmore et al.

BMC Research Notes , 22 Aug 2008

Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics: Background The histone H3/H4 chaperone Asf1 (anti-silencing function 1) is required for the establishment and maintenance of proper chromatin structure, as well as for genome stability in eukaryotes. Asf1 participates in both DNA replication-coupled (RC) and replication-independent (RI) histone deposition reactions in vitro and interacts with complexes responsible for both pathways in vivo . Asf1 is known to directly bind histone H3, however, high-resolution structural information about the geometry of this interaction was previously unknown. Results Here we report the structure of a histone/histone chaperone interaction. We have solved the 2.2 Å crystal structure of the conserved N-terminal immunoglobulin fold domain of yeast Asf1 (residues 2–155) bound to the C-terminal helix of yeast histone H3 (residues 121–134). The structure defines a histone-binding patch on Asf1 ...

Andrew J Antczak et al.

BMC Structural Biology , 13 Dec 2006

The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein: ... at least in part, by a histone deacetylase complex, whose enzymatic activity relies on HDAC1, HDAC2 or HDAC3. Recently, we have shown that the Rb-associated histone deacetylase complex contains RbAp48 protein, which interacts with HDAC1 and HDAC2. RbAp48 could favour the deacetylation of histones since it binds directly to histone H4. In agreement with that, we show that transcriptional repression of E2F activity requires the presence of RbAp48. HDAC3 was thought not to interact with RbAp48. However, we found that it shared with HDAC1 the ability to favour the recruitment of RbAp48 to Rb. This latter effect was unlikely to be due to activation of Rb function, since HDAC3 did not increase Rb–E2F1 interaction. Rather, we found, surprisingly, that HDAC3 could physically interact with RbAp48 both in vitro and in living cells. Taken together, our data suggest a model in which Rb mediates the recruitment to E2F-regulating promoters of a repressive complex containing either HDAC1, HDAC2 or HDAC3 and the histone-binding protein RbAp48.

Estelle Nicolas et al.

Nucleic Acids Research , 01 Aug 2001

TSPY potentiates cell proliferation and tumorigenesis by promoting cell cycle progression in HeLa and NIH3T3 cells: ... of cyclin B and/or histone binding proteins represented by ...

Shane W Oram et al.

BMC Cancer , 09 Jun 2006