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Proteins can treat defects in other proteins, shows study

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In a first ever discovery, the scientists have found that the proteins’ building blocks can be assembled without getting instructions from the DNA or the messenger RNA (mRNA).

In a new study, the researchers discovered a new protein, Rqc2, which played a significant role just like mRNA and also specified which amino acids, which are the called building blocks of proteins, should be added in cell mechanism.

Adam Frost, assistant professor at University of California, said, “In this case, we have a protein playing a role normally filled by mRNA.”

According to the researchers, the significant findings offer greater opportunity for new therapies for treating neurodegenerative diseases like Alzheimer’s, Huntington’s, Amyotrophic lateral sclerosis (ALS) and many more.

Calling the findings as ‘surprising’, study’s first author Peter Shen said, “The discovery reflects how incomplete our understanding of biology is.”

Shen is doing postdoctoral fellowship in Biochemistry at the University of Utah.

For the new study, the researchers fine-tuned a technique known as cryo-electron microscopy in order to flash freeze followed by visualizing the quality control machinery in the active cells.

According to the study researchers, the ribosomes are machines on a protein assembly line that links amino acids together in a distinct order specified by the genetic code.

Generally, the ribosome is generally disassembled when something goes wrong and the blueprint is discarded, while the partly made protein is recycled.

The researchers said that the new study showed that prior to the recycling of incomplete protein, Rqc2 can prompt the ribosomes for the addition of just two of the total of 20 amino acids, i.e. threonine and alanine, over and over, as well as in any order.

The findings of the study were published in the journal Science.

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Filed Under: Technology & Research Tagged With: Adam Frost, amino acids, DNA, mRNA, Peter Shen, Protein, RNA, Rqc2, University of California

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