7O6N

Crystal structure of C. elegans ERH-2 PID-3 complex

Summary for 7O6N

• Entry DOI: 10.2210/pdb7o6n/pdb
• Related: 7O6L
• Descriptor: Enhancer of rudimentary homolog 2, Protein pid-3, FORMIC ACID, ... (4 entities in total)
• Functional Keywords: erh-2 pid-3 complex pirna processing petisco, protein binding
• Biological source: Caenorhabditis elegans; More
• Total number of polymer chains: 4
• Total formula weight: 32706.51

Authors

Falk, S.,Ketting, R.F. (deposition date: 2021-04-11, release date: 2021-08-25, Last modification date: 2024-01-31)

Primary citation

Perez-Borrajero, C.,Podvalnaya, N.,Holleis, K.,Lichtenberger, R.,Karaulanov, E.,Simon, B.,Basquin, J.,Hennig, J.,Ketting, R.F.,Falk, S.
Structural basis of PETISCO complex assembly during piRNA biogenesis in C. elegans .
Genes Dev., 35:1304-1323, 2021

PubMed Abstract: Piwi-interacting RNAs (piRNAs) constitute a class of small RNAs that bind PIWI proteins and are essential to repress transposable elements in the animal germline, thereby promoting genome stability and maintaining fertility. piRNAs (21U RNAs) are transcribed individually from minigenes as precursors that require 5' and 3' processing. This process depends on the PETISCO complex, consisting of four proteins: IFE-3, TOFU-6, PID-3, and ERH-2. We used biochemical and structural biology approaches to characterize the PETISCO architecture and its interaction with RNA, together with its effector proteins TOST-1 and PID-1. These two proteins define different PETISCO functions: PID-1 governs 21U processing, whereas TOST-1 links PETISCO to an unknown process essential for early embryogenesis. Here, we show that PETISCO forms an octameric assembly with each subunit present in two copies. Determination of structures of the TOFU-6/PID-3 and PID-3/ERH-2 subcomplexes, supported by in vivo studies of subunit interaction mutants, allows us to propose a model for the formation of the TOFU-6/PID-3/ERH-2 core complex and its functionality in germ cells and early embryos. Using NMR spectroscopy, we demonstrate that TOST-1 and PID-1 bind to a common surface on ERH-2, located opposite its PID-3 binding site, explaining how PETISCO can mediate different cellular roles.

PubMed: 34413138
DOI: 10.1101/gad.348648.121

Experimental method

X-RAY DIFFRACTION (2.17 Å)