Disease relevance of LOC396232

• Production of functional chick liver HMG 2a protein in Escherichia coli [1].

High impact information on LOC396232

• The interaction of high mobility group protein 1 (HMG 1) isolated from chicken erythrocytes with DNA has been characterized using the intrinsic tryptophan fluorescence of the protein as a probe [2].
• Fluorescent titrations indicate that the physical site size for HMG 1 binding on native DNA is approximately 14 base pairs (or 14 bases for binding to single-stranded DNA) [2].
• Mononucleosomes generated by mild digestion of erythrocyte chromatin with micrococcal nuclease were highly enriched in HMG-2a [3].
• In hepatocytes HMG2b is barely detectable and HMG2a is the major subtype [4].
• High mobility group protein HMG-I(Y) selectively binds to stretches of A.T-rich B-form DNA in vitro by recognition of substrate structure rather nucleotide sequence [5].

Biological context of LOC396232

• Comparison of the nucleotide sequences of cDNA coding for chick liver HMG 2a with pig thymus HMG 2 and human monocytic leukemia cell HMG 2 showed 70% homology [6].
• The association of proteins HMG-1 and -2 with the genome of hen oviduct nuclei was probed by a limited digestion with nucleases [7].
• The ratios HMG1/nucleosomal histone and HMG2/nucleosomal histone increased markedly at the end of spermiogenesis during the transition from nucleohistone to nucleoprotamine when nucleosomes are being disassembled [8].
• These results suggest that the decrease in the HMG 2a protein contents of the muscle and gizzard in the 70-day-old chicks may be largely due to the stimulation of HMG 2a protein degradation or the reduction of HMG 2a mRNA translation [9].
• Preferential phosphorylation of high mobility group protein 17 in vitro by a nuclear protein kinase [10].

Anatomical context of LOC396232

• Comparative structural analysis of high mobility group proteins from a variety of sources. Evidence for a high mobility group protein unique to avian erythrocyte nuclei [11].
• Changes in quantities of high-mobility-group protein 1 in oviduct cellular fractions after oestrogen stimulation [12].
• After administration of oestrogen to young chicks in vivo for 5 days, the quantity of HMG 1 is increased 4-fold in the cytosol, 3.5-fold in the microsomal fraction and 1.6-fold in the nuclear fraction [12].
• The contents of both HMG 2a and 2b proteins of liver, heart, brain, muscle and gizzard were abundant in the newly hatched chicks but their contents decreased significantly in those tissues of the 70-day-old chicks [9].
• The high mobility group chromosomal proteins HMG1 and HMG2 were not detectable in the nuclei of rooster spermatozoa [8].

Associations of LOC396232 with chemical compounds

• The nuclear suspension was centrifuged and the contents of proteins HMG-1 and -2 in the supernatant and sediment fractions were analysed by polyacrylamide-gel electrophoresis [7].
• The purified product showed the expected NH2-terminal sequence and the superhelical activity of circular DNA similar to the authentic HMG 2a isolated from chick liver [1].
• Cross-linking with a 'zero-length' cross-linker 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide and with a longer (cleavable) cross-linker dimethyl-3,3'-dithiobispropionimidate revealed an interaction of HMG1 and HMG2 with (or proximity to) core histones in both types of particles [13].

Physical interactions of LOC396232

• It is concluded that one molecule of HMG 1 or 2 binds to the 40 base pairs of linker DNA whereas the HMG 14 or 17 molecules associate with the nucleosomal core [14].

Other interactions of LOC396232

• In glandular stomach, liver and spleen, the relative contents of both HMG-1 and HMG-2 are markedly lower than in thymus and Bursa Fabricii [15].
• Two molecules of HMG 14 or 17 are accommodated by particles with 140 or 180 base pairs of DNA whereas HMG 1 or 2 are only bound by the larger specimens irrespective of the presence of HMG 14/17 [14].
• The ability of the chromosomal high mobility group protein HMG 2 to recognize supercoil-dependent structures within the chicken adult beta-globin gene was investigated by examining its ability to protect such sites from digestion by S1 nuclease [16].

Analytical, diagnostic and therapeutic context of LOC396232

• Molecular cloning of chick liver HMG 2a cDNA and developmental expression of HMG 2a mRNA [6].
• The nature of the binding of a high mobility group protein (HMG 17) to native and H1-H5-depleted chicken erythrocyte chromatin was studied, as a function of ionic strength, using circular dichroism and thermal denaturation techniques [17].
• Binding constants have been measured for the interaction of the protein HMG1 with native DNA, denatured DNA and a number of polynucleotides at near-physiological ionic strengths, using gel filtration and thermal denaturation [18].

References