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Phosphorylation of deinococcal RecA affects its structural and functional dynamics implicated for its roles in radioresistance of Deinococcus radiodurans.

Authors
  • Sharma, Dhirendra Kumar1
  • Siddiqui, Mohammad Quadir2
  • Gadewal, Nikhil2
  • Choudhary, Rajan Kumar2
  • Varma, Ashok Kumar2
  • Misra, Hari Sharan1, 3
  • Rajpurohit, Yogendra Singh1, 3
  • 1 Molecular Biology Division, Bhabha Atomic Research Centre, Mumbai, Maharashtra, India. , (India)
  • 2 Advance Centre for Treatment Research and Education in Cancer, Kharghar, Maharashtra, India. , (India)
  • 3 Department of Atomic Energy, Homi Bhabha National Institute, Mumbai, Maharashtra, India. , (India)
Type
Published Article
Journal
Journal of biomolecular structure & dynamics
Publication Date
Jan 01, 2020
Volume
38
Issue
1
Pages
114–123
Identifiers
DOI: 10.1080/07391102.2019.1568916
PMID: 30688163
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

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 77Communicated by Ramaswamy H. Sarma.

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