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Maurya, G. K.

Publications and source records attributed to Maurya, G. K..

2 recordsLinked to original sources

Overlapping oriC and centromere-like functions in secondary genome replicons determine their maintenance independent of chromosome I in Deinococcus radiodurans

The Deinococcus radiodurans multipartite genome system (MGS) consists of chromosome I (ChrI) and secondary genome elements; Chr II and megaplasmid (MP). The sequences upstream to parAB operons in Chr II (cisII) and MP (cisMP) helped an E. coli plasmid maintenance in D. radiodurans and showed sequence specific interactions with DnaA and ParBs. The cells devoid of cisII ({Delta}cisII) or cisMP ({Delta}cisMP) showed reduced {gamma} radiation resistance and copy number of Chr II and MP. Fluorescent Reporter-Operator System (FROS) developed for ChrI, ChrII and MP in {Delta}cisII or {Delta}cisMP mutants showed no change in wild type pattern of Chr I localization. However, the relative copy numbers of Chr II and MP had reduced while anucleate cells had increased in mutants. These results suggested that cisII and cisMP elements contain both ori and centromere-like functions, and like other MGS bacteria, the Chr I and secondary genome are maintained independently in D. radiodurans.

cell biology

PprA interacts with replication proteins and affects their physicochemical properties required for replication initiation in Deinococcus radiodurans

The deletion mutant of pprA, a gene encoding pleiotropic functions in radioresistant bacterium Deinococcus radiodurans, showed an increased genomic content and ploidy in chromosome I and chromosome II. We identified oriC in chromosome I (oriCI) and demonstrated the sequence specific interaction of deinococcal DnaA (drDnaA) with oriCI. drDnaA and drDnaB showed ATPase activity while drDnaB catalyzed 5'[->]3' dsDNA helicase activity. These proteins showed both homotypic and heterotypic interactions. The roles of C-terminal domain of drDnaA in oriCI binding and its stimulation of ATPase activity were demonstrated. Notably, PprA showed ~2 times higher affinity to drDnaA as compared to drDnaB and attenuated both homotypic and heterotypic interactions of these proteins. Interestingly, the ATPase activity of drDnaA but not drDnaB was inhibited in presence of PprA. These results suggested that PprA influences the physicochemical properties of drDnaA and drDnaB that are required for initiation of DNA replication at oriCI site in this bacterium.

molecular biology