Functional characterization of a hypothetical protein (TTHA1873) from Thermus thermophilus

被引:1
|
作者
Iyyappan, Yuvaraj [1 ,2 ]
Dhayabaran, Vaigundan [3 ]
Elayappan, Mohanapriya [1 ]
Chaudhary, Santosh Kumar [1 ,4 ]
Palaniappan, Chandrasekaran [1 ,5 ]
Kanagaraj, Sekar [1 ,6 ]
机构
[1] Indian Inst Sci, Dept Computat & Data Sci, Bangalore, India
[2] Natl Inst Plant Biotechnol, New Delhi, India
[3] Sri Devaraj Urs Acad Higher Educ & Res, Dept Cell Biol & Mol Genet, Genom & Cent Res Lab, Kolar, India
[4] Broad Inst & Harvard, Chem Biol & Therapeut Sci, Cambridge, MA USA
[5] Indian Inst Sci, Mol Biophys Unit, Bangalore, India
[6] Indian Inst Sci, Dept Computat & Data Sci, Bangalore 560012, India
关键词
CRISPR associated protein; DNA-relaxing activity; DNase; hypothetical protein; TTHA1873; DNA-LIGASE; EVOLUTIONARY CLASSIFICATION; HYPERTHERMOPHILIC ARCHAEON; RNA RECOGNITION; ATP-BINDING; MOTIF; ANNOTATION; EXPRESSION; DIVERSITY; SYSTEMS;
D O I
10.1002/prot.26530
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Thermus thermophilus is an extremely thermophilic organism that thrives at a temperature of 65 degrees C. T. thermophilus genome has similar to 2218 genes, out of which 66% (1482 genes) have been annotated, and the remaining 34% (736 genes) are assigned as hypothetical proteins. In this work, biochemical and biophysical experiments were performed to characterize the hypothetical protein TTHA1873 from T. thermophilus. The hypothetical protein TTHA1873 acts as a nuclease, which indiscreetly cuts methylated and non-methylated DNA in divalent metal ions and relaxes the plasmid DNA in the presence of ATP. The chelation of metal ions with EDTA inhibits its activity. These results suggest that the hypothetical protein TTHA1873 would be a CRISPR-associated protein with non-specific DNase activity and ATP-dependent DNA-relaxing activity.
引用
收藏
页码:1427 / 1436
页数:10
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