Fig. 8: Model of the role of Pla1 in MTREC-mediated degradation of CUTs. | Nature Communications

Fig. 8: Model of the role of Pla1 in MTREC-mediated degradation of CUTs.

From: Mechanistic insights into RNA surveillance by the canonical poly(A) polymerase Pla1 of the MTREC complex

Fig. 8: Model of the role of Pla1 in MTREC-mediated degradation of CUTs.The alternative text for this image may have been generated using AI.

MTREC complex is recruited to CUTs and meiotic mRNAs during their transcription by a not well understood mechanism. Pla1, as part of the CPF, is responsible for the initial poly-adenylation of CUTs and the resulting poly(A) tail is likely bound by the canonical poly(A) binding protein Pabp. MTREC complex sequesters Pla1 from CPF via Red1, replacing Iss1 that anchors Pla1 to CPF. MTREC-bound Pla1 hyper-adenylates CUTs. We suggest that the non-canonical poly(A)-binding protein, Pab2, might be preferentially loaded on these poly(A) tail extensions (marked with a "?" in the Fig.) to facilitate exosome-mediated degradation of CUTs. Both the CPF complex and the Red1-Pla1 interaction are required for the efficient recruitment of the ClrC complex to methylate histone H3K9 at meiotic heterochromatic islands, indicating a sophisticated functional interplay between CPF and MTREC complex during the transcriptional termination, end-processing and degradation of CUTs.

Back to article page