Protein splicing
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- Опубліковано 14 жов 2024
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Protein splicing is an intramolecular reaction of a particular protein in which an internal protein segment (called an intein) is removed from a precursor protein with a ligation of C-terminal and N-terminal external proteins (called exteins) on both sides. The splicing junction of the precursor protein is mainly a cysteine or a serine, which are amino acids containing a nucleophilic side chain. The protein splicing reactions which are known now do not require exogenous cofactors or energy sources such as adenosine triphosphate (ATP) or guanosine triphosphate (GTP). Normally, splicing is associated only with pre-mRNA splicing.
The type of the splicing proteins is categorized into four classes: maxi-intein, mini-intein, trans-splicing intein, and alanine intein. The maxi-inteins are N- and C-terminal splicing domains containing an endonuclease domain. The mini-inteins are typical N- and C-terminal splicing domains; however, the endonuclease domain is not present. The trans-splicing inteins are split inteins which are divided into N-termini and C-termini. Alanine inteins have the splicing junction of an alanine instead of a cysteine or a serine, in both of which the protein splicing occurs.
Good point about Inteins being the selfish elements!
so u mean to say that protein splicing does'nt occur in bacteria as it will die???
Why can the nucleophilic side-chain not be threonine as well as serine or cysteine? I can see why tyrosine might not work as it might be hard for it to reach the carbon it needs to attack, but threonine is quite similar to serine...
Thr can be used in some cases. It depends on the intein being employed.
You should make a more detailed video on this topic
Excellent vai
so is the existence of this mechanism just a hypothesis in prokaryotes?
You are the so inspiring me and well taught
You're welcome
Superb se bhi uper
Thank you
thank you sir..