標題: Staphylococcus aureus protein SAUGI acts as a uracil-DNA glycosylase inhibitor
作者: Wang, Hao-Ching
Hsu, Kai-Cheng
Yang, Jinn-Moon
Wu, Mao-Lun
Ko, Tzu-Ping
Lin, Shen-Rong
Wang, Andrew H. -J.
生物科技學系
生物資訊及系統生物研究所
Department of Biological Science and Technology
Institude of Bioinformatics and Systems Biology
公開日期: 1-一月-2014
摘要: DNA mimic proteins are unique factors that control the DNA binding activity of target proteins by directly occupying their DNA binding sites. The extremely divergent amino acid sequences of the DNA mimics make these proteins hard to predict, and although they are likely to be ubiquitous, to date, only a few have been reported and functionally analyzed. Here we used a bioinformatic approach to look for potential DNA mimic proteins among previously reported protein structures. From similar to 14 candidates, we selected the Staphylococcus conserved hypothetical protein SSP0047, and used proteomic and structural approaches to show that it is a novel DNA mimic protein. In Staphylococcus aureus, we found that this protein acts as a uracil-DNA glycosylase inhibitor, and therefore named it S. aureus uracil-DNA glycosylase inhibitor (SAUGI). We also determined and analyzed the complex structure of SAUGI and S. aureus uracil-DNA glycosylase (SAUDG). Subsequent BIAcore studies further showed that SAUGI has a high binding affinity to both S. aureus and human UDG. The two uracil-DNA glycosylase inhibitors (UGI and p56) previously known to science were both found in Bacillus phages, and this is the first report of a bacterial DNA mimic that may regulate SAUDG's functional roles in DNA repair and host defense.
URI: http://dx.doi.org/10.1093/nar/gkt964
http://hdl.handle.net/11536/23856
ISSN: 0305-1048
DOI: 10.1093/nar/gkt964
期刊: NUCLEIC ACIDS RESEARCH
Volume: 42
Issue: 2
起始頁: 1354
結束頁: 1364
顯示於類別:期刊論文


文件中的檔案:

  1. 000331138100058.pdf