Understanding how phosphates affect proteins
Deep within the cellular structure of all living organisms, chemical reactions are taking place. These reactions control biological events and are part of the processes that regulate metabolism, gene expression and cell division, as well as growth, development, motion, learning and memory.
Proteins in living cells "talk" to each other. One of the most common forms of communication involves adding or removing phosphate groups to and from proteins. Protein phosphorylation—the addition of a phosphate to a protein—is a critically important regulatory mechanism. Much like attaching a switch to a light bulb, adding a phosphate group to a protein can turn the protein on or off and triggers its biological activity.
While protein phosphorylation has been extensively studied in mammals, research lags in lower organisms such as bacteria. What’s more, some “atypical” human kinases (which are similar to canonical kinases but feature significant difference) are also understudied. A kinase is also known as an enzyme.
Zongchao Jia, Canada Research Chair in Structural Biology, has been examining the bacteria kinases that are involved in stress response such as limited nutrition conditions and exposure to antibiotics, in addition to studying human atypical kinases.
Jia is using crystallography, a powerful research technique that can provide direct visualization of the three-dimensional structure of a protein. Based on the "picture" he obtains, Jia is able to uncover important functional insights into these kinases.
Jia’s research will improve knowledge of kinases that are uniquely found in bacteria and humans. This may lead to the development of selective antibiotics and therapeutics in the future.