| MG-I and HMG-Y are members of the high mobility group of non-histone chromosomal proteins. These proteins are unique in that they specifically bind to A + T-rich stretches of DNA and that they are found predominantly in rapidly dividing, undifferentiated or neoplastic cells.;Amino acid sequence analysis of purified HMG-Y indicates that it is identical to HMG-I except that it is missing an internal stretch of eleven contiguous amino acids. This, along with nucleic acid sequence data, suggest that HMG-I and HMG-Y are encoded by the same gene but that differential processing of the gene's cognate mRNA produces two isoform proteins.;Analysis of a crude nuclear extract from lymphoid derived ascites cells reveals that it contains a protein, which was identified as HMG-I, that binds specifically to the 3;The effects of the sequence specific binding of HMG-I(Y) with the bovine interleukin-2 cDNA have been studied. HMG-I(Y) binding alters the structure of the cDNA, as determined by circular dichroism analysis, and stabilizes the cDNA against thermodenaturation.;A putative genomic human HMG-Y clone was obtained by using a HMG-Y cDNA to probe a human EMBL-3 genomic library. Sequence analysis of the clone revealed that it is... |
