Researchers at Johns Hopkins took advantage of a new technique that reads the makeup of proteins to identify nearly all chemical changes nature makes by adding phosphate to proteins manufactured in human cells.

The Hopkins team then added its list of these so-called phosphorylation events to lists compiled by others and created a publicly available database on the Web - PhosphoMotif Finder [ http://www.hprd.org/PhosphoMotif_finder ] - to help speed the work of researchers around the world.

Finding so many at one time is a huge advance, says Akhilesh Pandey, M.D., Ph.D., an associate professor at the McKusick-Nathans Institute of Genetic Medicine at Hopkins. Phosphorylation is essential for controlling chemical reactions in our cells protein factories, and phosphorylation gone awry has been implicated in several diseases. The ability to study more than one phosphorlyation at a time will help us understand some of these diseases - including cancers - sooner.

What we have here is about 20 years worth of lots of work in one searchable list, says Pandey. A report on all of the newly identified protein alterations is published in the Feb. 13 issue of the Proceedings of the National Academy of Sciences, while a report on the database appears in the March issue of Nature Biotechnology.

Pandeys team used electron transfer dissociation (ETD) tandem mass spectrometry, a technology that breaks apart proteins into small fragments, separates them by size and identifies the fragments based on their mass - their size and weight. The process improves on previous techniques by breaking up proteins more gently and keeping chemical modifications like phosphorylation intact. Previous spectrometry methods were just too rough on the delicate protein alterations and sheared them right off, he says. We had to guess where they might be and nobody wants to chase false leads based on wrong gues
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Contact: Audrey Huang
audrey@jhmi.edu
410-614-5105
Johns Hopkins Medical Institutions
22-Apr-2007