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Prp24
Prp24 (precursor RNA processing, gene 24) is a protein part of the pre-messenger RNA splicing process and aids the binding of U6 snRNA to U4 snRNA during the formation of spliceosomes. Found in eukaryotes from yeast to ''E. coli'', fungi, and humans, Prp24 was initially discovered to be an important element of RNA splicing in 1989. Mutations in Prp24 were later discovered in 1991 to suppress mutations in U4 that resulted in cold-sensitive strains of yeast, indicating its involvement in the reformation of the U4/U6 duplex after the catalytic steps of splicing.
==Biological Role==
The process of spliceosome formation involves the U4 and U6 snRNPs associating and forming a di-snRNP in the cell nucleus. This di-snRNP then recruits another member (U5) to become a tri-snRNP. U6 must then dissociate from U4 to bond with U2 and become catalytically active. Once splicing has been done, U6 must dissociate from the spliceosome and bond back with U4 to restart the cycle.
Prp24 has been shown to promote the binding of U4 and U6 snRNPs. Removing Prp24 results in the accumulation of free U4 and U6, and the subsequent addition of Prp24 regenerates U4/U6 and reduces the amount of free U4 and U6. Naked U6 snRNA is very compact and has little room to form base pairs with other RNA. However, when U6 snRNP associates with proteins such as Prp24, the structure is much more open, thus facilitating the binding to U4. Prp24 is not present in the U6/U4 duplex itself, and it has been suggested that Prp24 must leave the complex in order for proper base pairs to be formed. It has also been suggested that Prp24 may play a role in destabilizing U4/U6 in order for U6 to pair bases with U2.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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