Jaiswal, Sanjay KumarVaishampayan, AkhouriSingh, Vinay KumarVaishampayan, AkhouriDhar, BanshiDakora, Felix Dapare2024-11-042024-11-042013-12-191590-4261 (P)1869-2044 (E)http://dx.doi.org/10.1007/s13213-013-0796-5https://hdl.handle.net/20.500.14519/1011The ability to rapidly adapt to changes in their environment is essential for the survival of microorganisms. DnaK is the prokaryotic analogue of eukaryotic Hsp70. These proteins protect the cell against heat injury or other forms of stress. In the present research, 78 rhizobial isolates were collected from different geographical regions of India and tested for their sensitivity. Forty-two out of 78 were shown to be susceptible to eight isolated phages. Only six Rhizobium strains out of 42 (MPSR033, MPSR041, MPSR052, MPSR084, MPSR220 and UPSR095) showed susceptibility to a single phage strain separately. All of these six rhizobial strains were slow growing and had the capability of Ex-planta nitrogenase activities. The PCR amplification of the dnaK region of the selected strain showed a single band~ 600 bp in length. The restriction endonuclease analysis of dnaK regions produced six restriction patterns. Sequence BLASTn analysis of DnaK showed linkage with Actinobacterium sp. and Bradyrhizobium sp. Multiple sequence alignment of all six Rhizobium dnaK regions exhibited a 99 % similarity betweenMPSR041 andMPSR220 and formed a close cluster with UPSR095 and MPSR033. The Prosite database showed that the functional domain of the DnaK protein presented three signatures, PS00297 IDLGTTNS (HSP70_1), PS00329 VYDLGGGTFDISIL (HSP70_2) and PS01036 VVLVGGMSRMPKVQE (HSP70_3), which belong to the HSP70 protein family. An in-silico interaction study revealed that DnaK protein is involved in interactions with blr, gap, grpE, pgk, hrcA and recA heat-shock proteins.1535–1542 PagesenAttribution-NonCommercial-ShareAlike 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-sa/4.0/BradyrhizobiumDnaKProteinInteractionArticle