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Home » Biology Articles » Biochemistry » Revealing the Secret of How Enzymes Differentiate Cellular Messages

Revealing the Secret of How Enzymes Differentiate Cellular Messages

Now and then, we forced ourselves to sort the things at hand, like the news paper, the news messages in our mailbox, or even the advertising files; we are slow to just throw them all in the trash or delete them before we read all of them in case of missing any important information.

Interestingly, so do the proteins in the cell. They read through the messages and decide what to be important and what to be trash. However, those messages are always at a mess, while some messages carry significant information. So how does the protein distinguish those differences? With those questions in mind, scientists had done numerous researches and found that there’s a protein called DIS3L2 which uses a multitude of recognition sites to figure out messages that are marked for destroy.

Now and then, we forced ourselves to sort the things at hand, like the news paper, the news messages in our mailbox, or even the advertising files; we are slow to just throw them all in the trash or delete them before we read all of them in case of missing any important information.

DIS3L2 is a molecular that helps maintain the identity of stem cells, protecting them from changing into other types. It achieves this like a goalkeeper, cutting the messages up until they don’t encode any useful information of the stem cells any more. On the one hand, DIS3L2 has to degrade those messages that would change the fate of the stem cells; on the other hand, the devastating consequences would be far beyond imagination if messages were cut up wrong. So, DIS3L2 should be specific, thus it only targets specific messages that have been marked by “poly-U” chain. In addition, the enzyme ignores most of the messages in the cell which go on to encode proteins and other useful information with the ends decorated with “poly-A”.

So, there’s another question: how can DIS3L2 be able to distinguish between those two chains? A work once published on Nature had used X-ray crystallography to observe the structure of DIS3L2 when it was bounded to a poly-U chain. There, they saw the enzyme looked like a funnel, in which the poly-U chain inserted itself deeply and other messages remained in the top. For enzyme to read the poly-U chain, there’s a sticky web formed by a dozen contacts that hold the poly-U chain deeply in the enzyme, and other chains just slide out. According to the scientists, any corruption of these steps would lead to disorders and even cancer.

 

Reference:  

Christopher R. Faehnle, Jack Walleshauser, & Leemor Joshua-Tor. 03 August 2014. Mechanism of Dis3l2 substrate recognition in the Lin28–let-7 pathway. Nature (2014) doi:10.1038/nature13553. URL: http://www.nature.com/nature/journal/vaop/ncurrent/full/nature13553.html

 

This is written by Caroline from Creative Biomart, which is a world leading biotech company. 


rating: 5.00 from 4 votes | updated on: 23 Aug 2014 | views: 3401 |

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