nonhistone protein

nonhistone protein

[nän¦hi‚stōn ′prō‚tēn]
(biochemistry)
A class of acidic proteins in the cell nucleus associated with deoxyribonucleic acid.
References in periodicals archive ?
Histone and nonhistone protein acetylation regulates also normal hematopoiesis [58, 59], being a network of epigenetic regulators, including NuA4/p300/CBP/HBO1, needed for normal and hematopoietic development [60].
Similarly, acetylation of the nonhistone protein, [alpha]-Tubulin, also increased with increasing LBH589 concentrations (Figure 1(c), Supplementary Figure 1).
Sirt1 was reported to deacetylate various nonhistone protein targets, including p53, NF-[kappa]B, [beta]-catenin, and FoxO3a [32-34].
NCL is a nucleolar phosphoprotein that is also among the most abundant nonhistone proteins in the nucleus.
Chromatin is made up of DNA and histones as well as nonhistone proteins, which condenses DNA into the nucleus of a cell [3].
Therefore, the reason for using a serum of a primary Sjogren's syndrome with CCP antibody and positive for anti-Ro60 and anti-La antibodies, as well as the lack of commercial antibodies against citrullinated nonhistone proteins, encouraged us to purify CCP antibodies to identify possible areas of citrulination in parotids of Balb/c mice, since the human CCP antibodies have been successfully used by others for tissue labelling [40].
Silent information regulator 1 (SIRT1), an [NAD.sup.+]-dependent deacetylase, is known to deacetylate histone and nonhistone proteins such as transcription factors.
The enzymatic acetylation of proteins is largely confined to acetyl CoA-dependent acetylation of histones [3, 5, 6] and nonhistone proteins [2, 4, 7] by specific acetyltransferases known as HATs.
Experiments discriminating between the possibilities that H1.2 displacement may be a response to acetylation-dependent changes of chromatin organization vis-a-vis effects on histones or by the modulation of nonhistone proteins would provide additional insight into this regulation.
Histone acetyltransferases (HATs) enzymes regulate the acetylation of histones and nonhistone proteins. The acetylation of the ?-amino groups of lysine residues present at histone tails correlates largely with transcriptional activation, but it is also involved in DNA replication, DNA repair and protein-protein interactions.
Histone proteins are found in association with multiple DNA regions throughout the chromosomes, whereas other nonhistone proteins (called "transcription factors") are characterized by DNA-binding segments that enable them to attach to target nucleotide sequences and regulate the transcription of specific genes.