Structural basis for RNA 3'-end recognition by the PIWIL2 PAZ domain

Qianqian Li; Aiping Dong; Zhongliang Zhu; Jiahai Zhang; Yanjun Li; Chao Xu

doi:10.1016/j.bbrc.2021.03.080

Structural basis for RNA 3'-end recognition by the PIWIL2 PAZ domain

Biochem Biophys Res Commun. 2021 May 14:553:187-190. doi: 10.1016/j.bbrc.2021.03.080. Epub 2021 Mar 25.

Authors

Qianqian Li¹, Aiping Dong², Zhongliang Zhu¹, Jiahai Zhang¹, Yanjun Li², Chao Xu³

Affiliations

¹ MOE Key Laboratory for Membraneless Organelles and Cellular Dynamics, Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, 230027, China.
² Structural Genomics Consortium, University of Toronto, 101 College St., Toronto, Ontario, M5G 1L7, Canada.
³ MOE Key Laboratory for Membraneless Organelles and Cellular Dynamics, Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, 230027, China. Electronic address: xuchaor@ustc.edu.cn.

PMID: 33774220
DOI: 10.1016/j.bbrc.2021.03.080

Abstract

PIWI family proteins are important members of Argonaute family that play an essential role in spermatogenesis and development when loaded with piRNAs. Here we solved the crystal structure of the human PIWIL2 PAZ domain and found its PAZ domain adopts a canonical PAZ fold. We furhter built a homology model of PIWIL2 bound to 2 nt 3' overhangs. We found that PIWIL2 utilizes a deep hydrophobic concave to accommodate the 2 nt at 3'-end of RNAs. The recognition of 2 nt 3' overhangs by PIWIL2 is conserved in other human PIWIL proteins, implicating the evolutionarily conserved role of PAZ domain in binding to target RNAs.

Keywords: PAZ domain; PIWI proteins; RNAi; Structure; piRNA.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Argonaute Proteins / chemistry*
Argonaute Proteins / metabolism
Binding Sites
Crystallography, X-Ray
Humans
Hydrophobic and Hydrophilic Interactions
Models, Molecular
Protein Domains
Protein Folding

Substances

Argonaute Proteins
PIWIL2 protein, human