Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Mammalian PIWI-piRNA-target complexes reveal features for broad and efficient target silencing.
Journal, issue, pages	Nat Struct Mol Biol, Year 2024
Publish date	Apr 24, 2024
Authors	Zhiqing Li / Zhenzhen Li / Yuqi Zhang / Lunni Zhou / Qikui Xu / Lili Li / Lin Zeng / Junchao Xue / Huilin Niu / Jing Zhong / Qilu Yu / Dengfeng Li / Miao Gui / Yongping Huang / Shikui Tu / Zhao Zhang / Chun-Qing Song / Jianping Wu / En-Zhi Shen /
PubMed Abstract	The PIWI-interacting RNA (piRNA) pathway is an adaptive defense system wherein piRNAs guide PIWI family Argonaute proteins to recognize and silence ever-evolving selfish genetic elements and ensure ...The PIWI-interacting RNA (piRNA) pathway is an adaptive defense system wherein piRNAs guide PIWI family Argonaute proteins to recognize and silence ever-evolving selfish genetic elements and ensure genome integrity. Driven by this intensive host-pathogen arms race, the piRNA pathway and its targeted transposons have coevolved rapidly in a species-specific manner, but how the piRNA pathway adapts specifically to target silencing in mammals remains elusive. Here, we show that mouse MILI and human HILI piRNA-induced silencing complexes (piRISCs) bind and cleave targets more efficiently than their invertebrate counterparts from the sponge Ephydatia fluviatilis. The inherent functional differences comport with structural features identified by cryo-EM studies of piRISCs. In the absence of target, MILI and HILI piRISCs adopt a wider nucleic-acid-binding channel and display an extended prearranged piRNA seed as compared with EfPiwi piRISC, consistent with their ability to capture targets more efficiently than EfPiwi piRISC. In the presence of target, the seed gate-which enforces seed-target fidelity in microRNA RISC-adopts a relaxed state in mammalian piRISC, revealing how MILI and HILI tolerate seed-target mismatches to broaden the target spectrum. A vertebrate-specific lysine distorts the piRNA seed, shifting the trajectory of the piRNA-target duplex out of the central cleft and toward the PAZ lobe. Functional analyses reveal that this lysine promotes target binding and cleavage. Our study therefore provides a molecular basis for the piRNA targeting mechanism in mice and humans, and suggests that mammalian piRNA machinery can achieve broad target silencing using a limited supply of piRNA species.
External links	Nat Struct Mol Biol / PubMed:38658622
Methods	EM (single particle)
Resolution	3.0 - 3.4 Å
Structure data	33797 7yfq EMDB-33797, PDB-7yfq: Cryo-EM structure of the EfPiwi (N959K)-piRNA-target ternary complex Method: EM (single particle) / Resolution: 3.2 Å 33800 7yfx EMDB-33800, PDB-7yfx: Cryo-EM structure of Hili in complex with piRNA Method: EM (single particle) / Resolution: 3.4 Å 33801 7yfy EMDB-33801, PDB-7yfy: Cryo-EM structure of the Mili-piRNA- target ternary complex Method: EM (single particle) / Resolution: 3.4 Å 33809 7yg6 EMDB-33809, PDB-7yg6: Cryo-EM structure of the EfPiwi(N959K) in complex with piRNA Method: EM (single particle) / Resolution: 3.2 Å 33817 7ygn EMDB-33817, PDB-7ygn: Cryo-EM structure of the Mili in complex with piRNA Method: EM (single particle) / Resolution: 3.0 Å
Chemicals	ChemComp-MG: Unknown entry
Source	ephydatia fluviatilis (invertebrata) homo sapiens (human) mus musculus (house mouse)
Keywords	RNA BINDING PROTEIN/RNA / piRNA / Piwi protein / Argonaute / RNA BINDING PROTEIN / RNA BINDING PROTEIN-RNA complex