A Review on the Mode of the Interactions of Bacterial Proteases with Their Substrates

Maintaining the quality of cellular proteome is a huge challenge to living cell as the proper functioning of protein directly affects proper functioning as well as survival of the cell. Due to different cellular stresses, the cellular proteins face recurring threats which has a negative impact on cellular proteins. As a result of these threats, proteins become damaged as well as misfolded, and these defective proteins impose a load to the cellular machinery by elevating the level of cytotoxicity. Protease enzymes are a type of cellular machinery that is specifically used to eliminate the damaged and short-lived regulatory proteins by their proteolytic mechanisms. Bacteria evolves different types of bacterial proteases that are highly diverse which correspond to their localization, sequence, structure, active sites, proteolytic mechanism, substrate specificity as well as function. Bacterial proteases not only eliminate the damaged protein but also act as chaperones in some special situation and thus act as charonin which makes a promising effect in cellular protein quality control. This study illustrates the detailed comparison of bacterial FtsH, Lon and Clp protease and their modes of interaction with substrates.