POP1 is a protein that has a key role in many nuclear complexes. It is most well known for being apart of the Ribonuclease P and MRP complexes. Ribonuclease P cleaves the 5’ end of pre-tRNA, and ribonuclease MRP cleaves pre -rRNA, both to generate the mature forms of their respective RNA form. POP1 has an integral role in these complexes.
Recently, POP1 has been implicated in the formation of the telomerase complex. It has been shown to stabilise TERC (the telomerase RNA component). When this goes wrong, it has been linked to breast cancer.
Structurally, there are two notable domains, an N-terminal motif and a C terminal domain. The first interacts with POP5, and the second interacts with RNA and other components of the ribonuclease P complex. In this model H1 RNA is used to illustrate this RNA interaction.
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