HMGN2

HMG protein is the most abundant non-histone family in the nucleus of vertebrates and invertebrates and is ubiquitous in higher eukaryotes. High mobility group protein N2 (HMGN2) is a member of the high mobility group family of proteins and is a novel antimicrobial peptide with an amphipathic a-helical structure that is ubiquitous in the nucleus of higher eukaryotic cells. HMGN2 belongs to the HMGN subfamily and has a relative molecular mass of about 9200. It consists of 90 amino acid residues and is a basic protein. It is a group of nuclear proteins that bind to nucleosomes and are expressed in the nucleus and cytoplasm. In the a-helical structure area. The coding gene of HMGN2 belongs to a multi-gene family. Only one of the functional genes in the HMGM2 multi-gene family was found by gene hybridization and located on chromosome 1P36.1. HMGN2 is a linear molecule containing no disulfide bond structure. The nucleosome binding region consisting of 17 to 47 and 30 amino acids encoded by exon 3 and exon 4 is a strong cationic region with nucleosome binding function. HMGN2 is anchored to the chromosome and analyzed as an a-helix region with transmembrane function.
Studies have shown that the expression of HMGN2 in tissues has certain specificity: HMGN2 mRNA is higher in the cards, liver, lung and thymus of human prostate, pituitary, thyroid, thymus, bone marrow and fetus, and the levels in other tissues are moderate. Amen et al found that HMGN2 can also be expressed in the oral cavity of the teeth and embryos of 14.5 d molars. In the epithelium, its expression is restricted by embryonic tissues, and the expression of HMGN2 is decreased in mature tissues. Due to the high conservation of HMGN2, early studies often extracted from bovine thymus or chicken red blood cells, so that the HMG proteins are well separated. Such extraction methods have rich sources and natural structures, but the disadvantages This is not the human HMGN2. Later, people tried to extract from human tumor cell lines and even induced the expression of the HMGN2 protein by molecular cloning. However, the HMGN2 obtained by this technique has no post-coding modification of the eukaryotic protein. Boumba et al. successfully extracted HMGN2 from porcine thymus and sequenced it. It found that its structure is the most similar to the homologous family protein derived from humans. It only has a conservative substitution at 64, ie, Tianmendong ammonia. The acid replaces glutamic acid.
In recent years, some scholars have successfully isolated and purified HMGN2 antimicrobial peptides from human monocytic cell line THP-1 cells.