Structural and interaction analysis of the Rrp5 C‐terminal region

Abstract

Rrp5 is an essential factor during the ribosome biogenesis process. The protein contains a series of 12 S1 RNA ‐binding domains followed by a TetratricoPeptide Repeat ( TPR ) domain. In the past, several studies aiming at defining the function of the TPR domain have used nonequivalent Rrp5 constructs, as these protein fragments include not only the TPR module, but also three or four S1 domains. We solved the structure of the Rrp5 TPR module and demonstrated in vitro that the TPR region alone does not bind RNA , while the three S1 domains preceding the TPR module can associate with homopolymeric RNA . Finally, we tested the association of our Rrp5 constructs with several proposed interactors, in support of cryo‐ EM ‐based models. Coordinates Atomic coordinates and structure factors have been deposited to the Protein Data Bank under the accession number 5NLG .

Programmed cell death 11 modulates but not entirely relies on p53-HDM2 loop to facilitate G2/M transition in colorectal cancer cells

“…PDCD11 reportedly regulates mature of 18S rRNA through protein-RNA interaction in the nucleolus [17]. Since most of the RNA binding sites were localized on the p53 binding domain (aa 1-1032) and HDM2binding domain (aa 1033-1431) of PDCD11 [16], a mass of RNA molecules might competitively inhibit PDCD11-p53/HDM2 interaction in the nucleolus. When in the nucleoplasm, PDCD11 is released from RNA binding and thereby performs its nonnucleolar function through binding to p53, HDM2, or other molecules.…”

“…PDCD11 (Gene ID: 22984) [12], also known as ALG-4 [13], RRP5 [14], or NFBP [15], is located on human chromosome 10q24.33, contains 37 exons, and encodes a translational product with 1871 amino acids. This protein possesses a series of S1 RNAbinding domains in the N-terminus with approximately 1,400 amino acids, followed by a tetratricopeptide repeat (TPR) domain in the C-terminus [16]. Through S1 N-terminal domains, PDCD11 interacts with pre-rRNA to coordinate rRNA processing and assembly in the nucleolus [14,[17][18][19].…”