Structure and function of eTudor domain containing TDRD proteins

Abstract

Tudor domain-containing (TDRD) proteins, as a family of evolutionarily conserved proteins, have been studied extensively in recent years in terms of their biological and biochemical functions. A major function of the TDRD proteins is to recognize the N-terminal arginine-rich motifs of the P-element-induced wimpy testis (PIWI) proteins via their conserved extended Tudor (eTudor or eTud) domains, which is essential in piRNA biogenesis and germ cell development. In this review, we summarize recent progress in the study of the TDRD proteins, and discuss the molecular mechanisms for the different binding selectivity of these eTudor domains to PIWI proteins based on the available binding and structural data. Understanding the binding differences of these TDRDs to PIWI proteins will help us better understand their functional differences and aid us in developing the target-specific therapeutics, because overexpression or mutations of the human TDRD proteins have been demonstrated to associate with various diseases.

Keywords:

• TDRD proteins
• eTudor domain
• PIWI
• dimethylated arginine
• piRNA pathway

Acknowledgements

Due to the limited space, we apologize to those whose original work could not be cited in this review.

Disclosure statement

The authors declare no conflicts of interest.

Additional information

Funding

This work was supported by the National Natural Science Foundation of China under Grant (Number 31770834 and 31300629); Natural Science Foundation of Hubei Province under Grant (Number 2017CFB513); Central China Normal University (CCNU) from the college’s basic research and operation of Ministry of Education (MOE) under Grant (Number CCNU2015A05055 and CCNU19KYZHSY15).