6u7v | pdb_00006u7v
xRRM structure of spPof8
Structural highlights
Function[POF8_SCHPO] RNA-binding protein required for assembly of the holoenzyme telomerase ribonucleoprotein (RNP) complex (PubMed:29422501, PubMed:29422503, PubMed:29422664). Specifically binds telomerase RNA ter1 and promotes assembly of ter1 with catalytic subunit trt1 (PubMed:29422501, PubMed:29422503). Telomerase is a ribonucleoprotein enzyme essential that copies new telomeric repeats onto chromosome ends and functions to maintain cell division (PubMed:29422501, PubMed:29422503, PubMed:29422664).[1] [2] [3] Publication Abstract from PubMedLong non-coding RNAs can often fold into different conformations. Telomerase RNA, an essential component of the telomerase ribonucleoprotein (RNP) enzyme, must fold into a defined structure to fulfill its function with the protein catalytic subunit (TERT) and other accessory factors. However, the mechanism by which the correct folding of telomerase RNA is warranted in a cell is still unknown. Here we show that La-related protein Pof8 specifically recognizes the conserved pseudoknot region of telomerase RNA and instructs the binding of the Lsm2-8 complex to its mature 3' end, thus selectively protecting the correctly folded RNA from exonucleolytic degradation. In the absence of Pof8, TERT assembles with misfolded RNA and produces little telomerase activity. Therefore, Pof8 plays a key role in telomerase RNA folding quality control, ensuring that TERT only assembles with functional telomerase RNA to form active telomerase. Our finding reveals a mechanism for non-coding RNA folding quality control. Quality-Control Mechanism for Telomerase RNA Folding in the Cell.,Hu X, Kim JK, Yu C, Jun HI, Liu J, Sankaran B, Huang L, Qiao F Cell Rep. 2020 Dec 29;33(13):108568. doi: 10.1016/j.celrep.2020.108568. PMID:33378677[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||||
