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Abstract
Proteins containing JAB1/MPN/MOV34 metalloenzyme (JAMM/MPN+) domains that have Zn2+-dependent deubiquitinase (DUB) activity are ubiquitous across among all domains of life. Recently, a homolog in Deinococcus radiodurans, DRJAMM, was reported to possess the ability to cleave DRMoaD-MoaE. However, the detailed biochemical characteristics of DRJAMM in vitro and its biological mechanism in vivo remain unclear. Here, we show that DRJAMM has an efficient in vitro catalytic activity in the presence of Mn2+, Ca2+, Mg2+, and Ni2+ in addition to the well-reported Zn2+, and strong adaptability at a wide range of temperatures. Disruption of drJAMM led to elevated sensitivity in response to H2O2 in vivo compared to the wild-type R1. In particular, the expression level of MoaE, a product of DRJAMM cleavage, was also increased under H2O2 stress, indicating that DRJAMM is needed in the antioxidant process. Moreover, DRJAMM was also demonstrated to be necessary for dimethyl sulfoxide respiratory system in D. radiodurans. These data suggest that DRJAMM plays key roles in the process of oxidative resistance in D. radiodurans with multiple-choice of metal ions and temperatures.
Highlights
Proteins containing JAMM/MPN+ domain (JAMMs) have been found in prokaryotes, eukaryotes, and archaea
When the amount of cyclic pyranopterin monophosphate (cPMP) was set to 100% in drJAMM mutant strain, it was not detected in wild-type R1 strain and drJAMM complementary strain (Supplementary Figure 1), indicating that DRJAMM is essential for the activation of DRMoaD-MoaE
These results suggested that the enzyme activity of DRJAMM has strong adaptability to a wide range of temperatures, even above 100◦C
Summary
Proteins containing JAMM/MPN+ domain (JAMMs) have been found in prokaryotes, eukaryotes, and archaea. They play important roles in all kinds of cellular processes such as DNA repair (Zeqiraj et al, 2015), pre-mRNA-processing (Galej et al, 2014), and sulfur mobilization to form molybdenum cofactors (Cao et al, 2015). The functional activity of zinc-dependent isopetidases involves zinc bound to the proteins via two histidines and one aspartic acid residues, such as AMSH (Davies et al, 2011) and CSN5 (Echalier et al, 2013), which are JAMM/MPN+ proteins and have the similar organization and composition. The proteins of the MPN− family lack catalytic activity due to the absence of pivotal residues in the typical JAMM motif and are usually found in pairs in multi-protein complexes with JAMM+
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