DRJAMM Is Involved in the Oxidative Resistance in .

Proteins containing JAB1/MPN/MOV34 metalloenzyme (JAMM/MPN) domains that have Zn-dependent deubiquitinase (DUB) activity are ubiquitous across among all domains of life. Recently, a homolog in , DRJAMM, was reported to possess the ability to cleave DRMoaD-MoaE. However, the detailed biochemical characteristics of DRJAMM and its biological mechanism remain unclear. Here, we show that DRJAMM has an efficient catalytic activity in the presence of Mn, Ca, Mg, and Ni in addition to the well-reported Zn, and strong adaptability at a wide range of temperatures. Disruption of led to elevated sensitivity in response to HO compared to the wild-type R1. In particular, the expression level of MoaE, a product of DRJAMM cleavage, was also increased under HO stress, indicating that DRJAMM is needed in the antioxidant process. Moreover, DRJAMM was also demonstrated to be necessary for dimethyl sulfoxide respiratory system in . These data suggest that DRJAMM plays key roles in the process of oxidative resistance in with multiple-choice of metal ions and temperatures.