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- 저자 : Tripti Anandan (검색결과 1 건)
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Phosphorylation Regulates Mycobacterial Proteasome
Tripti Anandan,Jaeil Han,Heather Baun,Seeta Nyayapathy,Jacob T. Brown,Rebekah L. Dial,Juan A. Moltalvo,Min-Seon Kim,양승환,Donald R. Ronning,Robert N. Husson,서주원,강충민 한국미생물학회 2014 The journal of microbiology Vol.52 No.9
Mycobacterium tuberculosis possesses a proteasome systemthat is required for the microbe to resist elimination by thehost immune system. Despite the importance of the proteasomein the pathogenesis of tuberculosis, the molecular mechanismsby which proteasome activity is controlled remainlargely unknown. Here, we demonstrate that the α-subunit(PrcA) of the M. tuberculosis proteasome is phosphorylatedby the PknB kinase at three threonine residues (T84, T202,and T178) in a sequential manner. Furthermore, the proteasomewith phosphorylated PrcA enhances the degradation ofIno1, a known proteasomal substrate, suggesting that PknBregulates the proteolytic activity of the proteasome. Previousstudies showed that depletion of the proteasome and the proteasome-associated proteins decreases resistance to reactivenitrogen intermediates (RNIs) but increases resistance tohydrogen peroxide (H2O2). Here we show that PknA phosphorylationof unprocessed proteasome β-subunit (pre-PrcB)and α-subunit reduces the assembly of the proteasome complexand thereby enhances the mycobacterial resistance toH2O2 and that H2O2 stress diminishes the formation of theproteasome complex in a PknA-dependent manner. Thesefindings indicate that phosphorylation of the M. tuberculosisproteasome not only modulates proteolytic activity of theproteasome, but also affects the proteasome complex formationcontributing to the survival of M. tuberculosis underoxidative stress conditions.
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