The proteins that are directly involved in PTMs of histones can be divided into three categories: the enzymes that create these modifications (the "writers"), the proteins that recognize the modifications (the "readers"), and the enzymes that remove the modifications (the "erasers").
In 2007, we introduced the use of small peptide loops that, upon binding of the hapten, specifically recognize the modifications of the antigen-binding site on the antibody, and therefore can be used to detect the formation of the immunocomplex (IC).
It can be explained that, actually, when n is too large, the enhancement influence on the output image is too slight, that is, it is difficult to recognize the modification in the overall brightness.
However, some regions in the enhanced image of the BPDHE method are dimmed unexpectedly with medium brightness pixels, while an enhancement of the RSWHE method is not strong enough to recognize the modification in the contrast.
Notably, the brain form of α-dystroglycan has a higher affinity for laminin-511/521 than its muscle counterpart, and the brain-specific mAb is thought to recognize the modification that binds to the LG domains of the laminin α5 chain.
Many so-called specific phosphotyrosine antibodies actually recognize the phosphotyrosine modification independently of its sequence context.
This is an important point, in that the same enzyme activities that are responsible for the acetylation/deacetylation of nucleosomal histones also acetylate/deacetylate those regulatory proteins that bind to chromatin and probably recognize the complex modification pattern established on nucleosomes.
Peptides that recognize the ubiquitous anticodon domain modification N-threonylcarbamoyladenosine can be used as a tool to study other modified tRNA protein interactions, for instance, those between tRNAs and their modification enzymes and/or aminoacyl-tRNA synthetases.
Various enzymes that are responsible for labeling and erasing the histone modifications ("writers") and proteins that specifically recognize these modifications ("readers") play a key role in the process of translating the "histone code" [4].
In this study, Tyr391 phosphorylation of human K19 was demonstrated by the use of a phospho-specific antibody recognizing the specific modification in PV-treated cells and mice.
A second enzyme, Lsp (lipotein signal peptidase), recognizes the diacylglyceryl modification and cleaves the leader sequence, when lipoproteins are translocated through the cytoplasmic membrane [63], resulting in the mature lipoprotein.
