{"id":2528,"date":"2015-07-02T00:00:00","date_gmt":"2015-07-02T07:00:00","guid":{"rendered":"https:\/\/vermont.salk.edu\/news-release\/new-technique-maps-elusive-chemical-markers-on-proteins\/"},"modified":"2015-11-15T08:18:45","modified_gmt":"2015-11-15T16:18:45","slug":"new-technique-maps-elusive-chemical-markers-on-proteins","status":"publish","type":"disclosure","link":"https:\/\/www.salk.edu\/es\/news-release\/new-technique-maps-elusive-chemical-markers-on-proteins\/","title":{"rendered":"Una nueva t\u00e9cnica permite localizar marcadores qu\u00edmicos dif\u00edciles de detectar en las prote\u00ednas"},"content":{"rendered":"

\nLA JOLLA\u2013Unveiling how the 20,000 or so proteins in the human body work\u2013and malfunction\u2013is the key to understanding much of health and disease. Now, Salk researchers developed a new technique that allows scientists to better understand an elusive step critical in protein formation.\n<\/p>\n

\nThe new method, described on July 2, 2015 in the journal C\u00e9lula<\/a><\/em>, allows researchers to map critical chemical tags\u2013called phosphates\u2013that bond to amino acids (the building blocks of proteins) in the final stages of creating a protein.\n<\/p>\n

\nWhen a cell produces a protein, molecular synthetic machinery first pieces together the amino acids into a long strand that bends and folds as it lengthens. Enzymes then gather around the structure to make final tweaks\u2013trimming the protein or adding chemical tags. Among these last modifications is phosphorylation\u2013or addition of phosphate\u2013of individual amino acids to change the protein\u2019s function. Until now, pinpointing exactly where (and why) all those phosphates are added has been tricky.\n<\/p>\n

\"\"<\/p>\n

\nSalk scientists developed antibodies that tag essential chemicals involved in protein action. In this dividing cell, the new antibody (green) marks discrete areas of a critical but elusive chemical reaction that happens when cells divide (DNA in blue and tubulin, a protein needed for cell division, in red).<\/p>\n

Haga clic aqu\u00ed<\/a> para obtener una imagen en alta resoluci\u00f3n.<\/p>\n

\nImagen: Cortes\u00eda del Instituto Salk de Estudios Biol\u00f3gicos\n<\/p>\n<\/div>\n

\n\u201cWe know that 9 out of the 20 amino acids can be phosphorylated, but we know very little about most of them because they\u2019re so hard to study,\u201d says Tony Hunter<\/a>, American Cancer Society<\/a> Professor, holder of the Dulbecco Chair in the Salk\u2019s Laboratorio de Biolog\u00eda Molecular y Celular<\/a> and senior author of the new paper.\n<\/p>\n

\nWhen phosphate is added to three particular amino acids\u2013serine, threonine and tyrosine\u2013it forms a strong chemical bond. Researchers can easily identify the location of these phosphates. But when the other six amino acids are phosphorylated, the phosphate is only loosely attached to each amino acid, causing problems for researchers trying to glean what happens in these cases. One of these amino acids, called histidine (or phosphohistidine once a phosphate is added), has been particularly tough to study.\n<\/p>\n

\n\u201cWith those strong phosphorylation events, you can label cells, isolate proteins and analyze the proteins in various ways to find out where the phosphates are,\u201d says Hunter. \u201cYou can\u2019t do that with phosphohistidine because it\u2019s so unstable it falls apart as you\u2019re trying to isolate the proteins.\u201d\n<\/p>\n

\nHunter and his collaborators realized that to study this unstable interaction, they would have to use a trick to make a stronger bond between phosphate and histidine. So they used a special kind of modified phosphate, called phosphonate, engineered to bind more tightly to either of the two spots on a histidine amino acid where phosphate can be added. Then, they developed antibodies that specifically recognize these stable phosphohistidine analogues, but also detect authentic phosphohistidine in proteins.\n<\/p>\n

\nTo test these new tools, the team added their phosphohistidine antibodies to a collection of different mammalian cells grown on slides and observed where in the cell the antibodies bound, which indicates parts of cells that have high levels of proteins with phosphohistidines.\n<\/p>\n

\n\u201cThe thing that surprised us most is that when we stained the cells with the new antibodies, we saw discrete areas within the cells that had high levels of histidine phosphorylation, particularly when they were undergoing mitosis, the stage at which cells divide into two daughter cells,\u201d says Hunter. They don\u2019t yet know exactly why that is, but plan to continue to explore these results as well as detect the phosphorylation of other amino acids.\n<\/p>\n

\nThe team expects these antibody tools to be useful to other labs aiming to determine whether proteins of interest have any phosphohistidines.\n<\/p>\n

\nThe new method is \u201cfairly easy for any lab to use,\u201d Hunter says. \u201cIt doesn\u2019t require a special instrument or anything, so I think it may be fairly quickly adopted.\u201d\n<\/p>\n

\nOther researchers on the study were Stephen Rush Fuhs, Jill Meisenhelder, Aaron Aslanian, Li Ma, Anna Zagorska and Greg Lemke<\/a>, of the Salk Institute; Magda Stankova, Alan Binnie, Fahad Al-Obeidi and Jacques Mauger, of Sanofi; and John R. Yates III of The Scripps Research Institute<\/a>.\n<\/p>\n

\nThe work and the researchers involved were supported by the Institutos Nacionales de Salud<\/a>, a Salk Institute Innovation Grant and the Helmsley Center for Genomic Medicine<\/a>.<\/p>","protected":false},"featured_media":0,"template":"","faculty":[72],"disease-research":[],"class_list":["post-2528","disclosure","type-disclosure","status-publish","hentry","faculty-tony-hunter"],"acf":[],"yoast_head":"\nNew technique maps elusive chemical markers on proteins - Salk Institute for Biological Studies<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/www.salk.edu\/es\/news-release\/new-technique-maps-elusive-chemical-markers-on-proteins\/\" \/>\n<meta property=\"og:locale\" content=\"es_MX\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"New technique maps elusive chemical markers on proteins - Salk Institute for Biological Studies\" \/>\n<meta property=\"og:description\" content=\"LA JOLLA\u2013Unveiling how the 20,000 or so proteins in the human body work\u2013and malfunction\u2013is the key to understanding much of health and disease. 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