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A new study by researchers at Penn State University reveals the chemical steps involved in adding an important tag—methyl sulfur group to transfer RNA.
Source: Booker Laboratory, Pennsylvania State University
A new study reveals the chemical steps of adding chemical tags to certain RNAs during important cell modifications
Related research results were published in the September 15th issue of Nature
Transfer RNA (tRNA) is an RNA that can "read" the genetic code and translate it into an amino acid sequence to make protein
"Methylthiolation is ubiquitous in bacteria, plants, and animals," said Squire Booker, a biochemist at Pennsylvania State University and a researcher at the Howard Hughes Medical Institute, who led the research team
The MiaB protein in Bacteroides uniform is a member of the Radical SAM (s-adenosylmethionine) enzyme family
Imaging the effects of MiaB and SAM molecules and tRNA at several points during the methylthiolation process allows researchers to infer the chemical steps in the modification process
"The source of the sulfur atom attached to the tRNA has always been controversial, but our structure shows that this methyl group and the sulfur attached to MiaB are eventually transferred to the tRNA, but before the tRNA accepts the methyl sulfide group, it will also happen.
The addition of an electron causes the second molecule of SAM to fragment into a free radical
Booker said: "Initially, the position of the hydrogen on the tRNA did not allow it to be close to both the free radical that removed it, and the methylsulfide group that needed to be transferred, because the hydrogen and the neighboring atoms are on the same plane
The result of these steps is a tRNA with methylthio added and successful modification
Next, the researchers hope to determine how the auxiliary cluster is rebuilt after each turnaround, and they are also studying similar proteins that play a similar role in the human modification process
(Biocom)
Original search:
Structural basis for tRNA methylthiolation by the radical SAM enzyme MiaB
DOI
10.
Structural basis of free radical SAM enzyme MiaB for methyl thiolation of tRNA
