Title

Sequence and structural analysis of 4SNc-Tudor domain protein from Takifugu Rubripes

Authors

Jianzhou Zheng¹, Jian Lu¹, Haijun Liu¹, Jun Li², Keping Chen^1,*

Affiliation

¹Institute of life science, Jiangsu University, Zhenjiang, China; ²Physical and Chemical Analysis Center, Jiangsu University, Zhenjiang, China

Email

kpchen@ujs.edu.cn

Article Type

Hypothesis

Date

Received April 01, 2009; Revised May 26, 2009; Accepted June 13, 2009; Published September 30, 2009

Abstract

The fugu SN4TDR protein belongs to an evolutionarily conserved family, consisting of four repeat staphylococcal nuclease-like domains (SN1-SN4) at the N-terminus followed by Tudor and SN-like domains (TSN). Sequence analysis showed that the C-terminal TSN domain is composed of a complete SN-like domain interdigitated with a Tudor domain. In despite of low level of sequence identities, five SN-like domains have a few conserved amino acids that may play essential roles in the function of the protein. Computer modeling and secondary structural prediction of the SN-like domains revealed the presence of similar structural features of β1-β2-β3-α1-β4-β5-α2-α3, which provides a structural basis for oligonucleotides binding. The loop region L3α for binding sites between β3 and α1 of SN-like domains are different from human p100, implying the divergence in the structures of binding sites. These results indicate that fugu SN4TDR may bind methylated ligands and/or oligonucleotides through its distant domains.

Takifugu rubripes, SN4TDR; SN-like domain; Tudor domain

Citation

Zheng et al., Bioinformation 4(3): 127-131 (2009)

Edited by

P. Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.