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The major histidine-rich glycoprotein (HRG) is a secreted protein that is found in mammals and their most distant relatives. HRG has been shown to be useful for the detection of breast and ovarian cancers. The high content of histidyl residues in HRG prompted us to search for other histidine-rich proteins in other species. We have identified a novel protein, which was here named the extended form of HRG (e-HRG), in a prokaryotic organism, Salmonella typhimurium. The e-HRG sequence has an overall amino acid identity of approximately 30% to the mammalian HRG protein. The similarity includes eight histidyl residues in the consensus sequence QXHXHX(3)X(3)H-GHH-R. E-HRG contains an amino-terminal signal peptide and a carboxy-terminal anchor, identical to those of mammalian HRG, as well as a third domain which is similar to the extracellular helix-3 of the immunoglobulins. The e-HRG gene was found in several prokaryotic species, including the S. typhimurium strain used in this study. The e-HRG gene is located on the chromosome which is organized into two operons; one contains the canonical HRG gene, while the other one has a new type of his-related gene, the HRG-like gene (HRGL), that appears to be a pseudogene. The e-HRG gene has received little attention despite its high level of conservation and highly expressed in prokaryotes. We believe that this work will lead to a better understanding of the evolutionary relationships among eukaryotic and prokaryotic histidine-rich glycoproteins.Xbox One Xbox One X Xbox One S Deals: November 1st, 2019
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