Abstract
Hfq, RNA binding protein, is widely found in most of the prokaryotes. It plays a key role in gene regulation by binding with small RNA and facilitates mRNA pairing there by suppress or boost translation according to RNA structures. Interaction between sRNAs and HfQ in Salmonella SL1344 were screened using Co-Immuno Precipitation (HfQ-CoIP) studies earlier. We have formulated an In silico approach, to model the 3D structures of 155 sRNA and studied their interactions with HfQ proteins. We have reported the key interacting PHE42, LEU7, VAL27, PHE39 and PRO21 residues of HfQ binds with many small RNAs. Further mutation of PHE42 in to ALA42 in HfQ leads to loss of sRNA binding efficiency. We have differentiated the interactions in to HfQ binding and non-binding sRNAs, based on Atomic Contact Energy and area. This methodology may be applied generically for functional grouping of small RNAs in any organism.