So.. as as significant blog post that you might be able to respond to, I will share a little background that hopefully is pretty clear on what the Hevel lab over in Widtsoe is all about.
The human body
is like a microscopic country. In order to properly function, all the different
locations must be able to communicate both globally and locally. Locally cells
use signaling pathways to detect and to respond to signals from the body.
Passing along a signal can be done chemically in many different ways; one way
is by enzymatically adding a small molecule to a protein to alter its function.
Many
significant physiological pathways, such as DNA repair, signal transduction,
and RNA processing are regulated by one such small modification known as
arginine methylation, where protein arginine methyltransferases (PRMTs) transfer a small methyl group onto an
arginine residue. This transfer can be done three ways; a single CH3
can be added to form monomethylarginine (MMA), two CH3 groups can be
added to different nitrogens to form symmetric dimethylarginine (SDMA), or two
CH3 groups can be added to the same nitrogen to form asymmetric
dimethylarginine (ADMA). Which product is formed has been observed to be
important for either activating or repressing the ability of a cell to use
certain pieces of its DNA. Understanding how PRMT1 targets its substrate(s)
lends vital information for drug development, often based on block the enzymes
ability to perform a key step in the pathway of choice.
Any questions or comments I can answer?
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