Pre-mRNA processing in eukaryotes involves capping, splicing, cleavage, and polyadenylation. Various proteins regulating this key transcriptional event in humans share considerable homology with Saccharomyces cerevisiae proteins. Among these proteins, Pcf11 is a crucial component of the yeast CF IA sub-unit, and Ydh1 is part of the CPF sub-unit. Both these proteins have a significant role during the pre-mRNA processing of the nascent transcription. Our in silico analysis highlights probable interaction between residues of Pcf11-Ydh1 and their role in mRNA processing events. These outcomes provide evidence for direct interaction between the domain from residues 116 to 204 of Pcf11 (Pcf11^116-204) with the N-terminal region of Ydh1 (residues 1-246; Ydh1^1-246). Molecular docking and MD simulations shed light on the structure and dynamics of the protein-protein complex that includes binding affinity and binding interface of Pcf11 and Ydh1 interaction. These outcomes would pave the way to further design in vitro and in vivo studies to determine the function of the Pcf11^116-204 domain, which has not been previously analyzed; this would also facilitate deciphering the crucial role of Ydh1 and Pcf11 in assembling the cleavage and polyadenylation complex for executing co-transcriptional processing to generate mature mRNA.

• PMID: 39660558
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Journal Article

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Kaur M, Arya H, Sharma A, Singh G, Kumar GS, Barnwal RP

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