Phosphorylation of deinococcal RecA affects its structural and functional dynamics implicated for its roles in radioresistance of Deinococcus radiodurans
| Autor: | Dhirendra K. Sharma, Mohammad Quadir Siddiqui, Yogendra S. Rajpurohit, Ashok K. Varma, Hari S. Misra, Rajan Kumar Choudhary, Nikhil Gadewal |
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| Rok vydání: | 2020 |
| Předmět: |
Functional dynamics
DNA repair Repair enzyme 030303 biophysics 03 medical and health sciences chemistry.chemical_compound Structural Biology Deinococcus radiodurans Deinococcus Threonine Tyrosine Phosphorylation Molecular Biology 0303 health sciences biology Chemistry Radioresistance General Medicine biology.organism_classification Cell biology Docking (molecular) bacteria DNA |
| Zdroj: | Datacite UnpayWall Microsoft Academic Graph Journal of Biomolecular Structure and Dynamics |
| DOI: | 10.1080/07391102.2019.1568916 |
| Popis: | Deinococcus RecA (DrRecA) protein is a key repair enzyme and contributes to efficient DNA repair of Deinococcus radiodurans. Phosphorylation of DrRecA at Y77 (tyrosine 77) and T318 (threonine 318) residues modifies the structural and conformational switching that impart the efficiency and activity of DrRecA. Dynamics comparisons of DrRecA with its phosphorylated analogues support the idea that phosphorylation of Y77 and T318 sites could change the dynamics and conformation plasticity of DrRecA. Furthermore, docking studies showed that phosphorylation increases the binding preference of DrRecA towards dATP versus ATP and for double-strand DNA versus single-strand DNA. This work supporting the idea that phosphorylation can modulate the crucial functions of this protein and having good concordance with the experimental data. AbbreviationsDrRecADeinococcus RecADSBDNA double-strand breakshDNAheteroduplex DNASTYPKserine/threonine/tyrosine protein kinaseT318threonine 318Y77tyrosine 77 Deinococcus RecA DNA double-strand breaks heteroduplex DNA serine/threonine/tyrosine protein kinase threonine 318 tyrosine 77 Communicated by Ramaswamy H. Sarma |
| Databáze: | OpenAIRE |
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