Disease relevance of LOC512161

• The HMG17-promoted DNA network formation has been observed with calf thymus type II DNA topoisomerase and the type I topoisomerases of Escherichia coli, Micrococcus luteus, and calf thymus [1].

High impact information on LOC512161

• This effect was observed with chromatin, but not with non-nucleosomal templates, and required the presence of HMG17 during chromatin assembly [2].
• HMG 14 and HMG 17 also contained minor sites which could be phosphorylated by cGMP-dependent protein kinase [3].
• Phosphorylation of HMG 17 in comparison was much less [4].
• We show further that reassociated HMG-17 molecules can exhibit a rapid interchange between binding sites, even under conditions of low ionic strength [5].
• Quantitative microcomplement fixation assays revealed that the indices of dissimilarity between HMG-1 and HMG-2, HMG-3, HMG-8, HMG-14, and HMG-17 were 2.0, 1.0, 3.8, 10.0, and 6.1, respectively [6].

Biological context of LOC512161

• In addition to HMG1, already known for its transfection activity, we have identified histone H1 and HMG17 as further transfection-active proteins [7].

Anatomical context of LOC512161

• The primary structure of the calf thymus non-histone chromosomal protein HMG-17 has been determined [8].
• We report the preparation of HMG17-containing oligonucleosomes from chicken embryos and from liver and oviduct of laying hens [9].

Associations of LOC512161 with chemical compounds

• The isolated proteins HMG 1, HMG 2 and HMG 17 from the tissues were compared by polyacrylamide-gel electrophoresis, isoelectric focusing and amino acid analysis [10].
• However, there are sequence similarities between HMG 18 and histone H5, and between HMG 19B and HMG 17, supporting the view that the HMG proteins and the lysine-rich histones are functionally related [11].

Other interactions of LOC512161

• Equal numbers of HMG-14 molecules can substitute for HMG-17 and generate the same nucleosome components [5].

Analytical, diagnostic and therapeutic context of LOC512161

• The conformation of the non-histone chromatin protein, HMG 17, has been studied using circular dichroism, infrared and nuclear magnetic resonance spectroscopies, and by small-angle scattering [12].
• The produced antiserum showed cross reactivity on blots and in inhibition ELISA with histone H1, even after its affinity purification with immobilized HMG-17 [13].
• We have used affinity chromatography to study the effects of phosphorylation of calf thymus high-mobility-group proteins HMG 14 and HMG 17 on their binding properties towards calf thymus single- and double-stranded DNA and histone H1 [14].

References