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

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. AbbreviationsDrRecA

Deinococcus RecA

DSB

DNA double-strand breaks

hDNA

heteroduplex DNA

STYPK

serine/threonine/tyrosine protein kinase

T318

threonine 318

Y77

tyrosine 77

Deinococcus RecA

DNA double-strand breaks

heteroduplex DNA

serine/threonine/tyrosine protein kinase

threonine 318

tyrosine 77

Communicated by Ramaswamy H. Sarma