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Legionella pneumophila SidD is a deAMPylase that modifies Rab1.

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  • المؤلفون: Tan Y;Tan Y; Luo ZQ
  • المصدر:
    Nature [Nature] 2011 Jul 06; Vol. 475 (7357), pp. 506-9. Date of Electronic Publication: 2011 Jul 06.
  • نوع النشر :
    Journal Article; Research Support, N.I.H., Extramural
  • اللغة:
    English
  • معلومة اضافية
    • المصدر:
      Publisher: Nature Publishing Group Country of Publication: England NLM ID: 0410462 Publication Model: Electronic Cited Medium: Internet ISSN: 1476-4687 (Electronic) Linking ISSN: 00280836 NLM ISO Abbreviation: Nature Subsets: MEDLINE
    • بيانات النشر:
      Publication: Basingstoke : Nature Publishing Group
      Original Publication: London, Macmillan Journals ltd.
    • الموضوع:
      Bacterial Proteins/*metabolism ; Legionella pneumophila/*enzymology ; Legionnaires' Disease/*enzymology ; rab1 GTP-Binding Proteins/*metabolism; Animals ; Aspartic Acid/chemistry ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/toxicity ; Cells, Cultured ; Female ; Guanine Nucleotide Exchange Factors/genetics ; Guanine Nucleotide Exchange Factors/metabolism ; Guanine Nucleotide Exchange Factors/toxicity ; Legionnaires' Disease/physiopathology ; Macrophages/enzymology ; Macrophages/pathology ; Mice ; Phenotype ; Plasmids/genetics ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae/metabolism ; Time Factors ; Transformation, Genetic
    • نبذة مختصرة :
      Legionella pneumophila actively modulates host vesicle trafficking pathways to facilitate its intracellular replication with effectors translocated by the Dot/Icm type IV secretion system (T4SS). The SidM/DrrA protein functions by locking the small GTPase Rab1 into an active form by its guanine nucleotide exchange factor (GEF) and AMPylation activity. Here we demonstrate that the L. pneumophila protein SidD preferably deAMPylates Rab1. We found that the deAMPylation activity of SidD could suppress the toxicity of SidM to yeast and is required to release Rab1 from bacterial phagosomes efficiently. A molecular mechanism for the temporal control of Rab1 activity in different phases of L. pneumophila infection is thus established. These observations indicate that AMPylation-mediated signal transduction is a reversible process regulated by specific enzymes.
    • Comments:
      Comment in: Cell Host Microbe. 2011 Aug 18;10(2):89-91. doi: 10.1016/j.chom.2011.08.002. (PMID: 21843863)
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    • Grant Information:
      R01AI069344 United States AI NIAID NIH HHS; R01 AI069344 United States AI NIAID NIH HHS; K02 AI085403-02 United States AI NIAID NIH HHS; K02AI085403 United States AI NIAID NIH HHS; R01 AI069344-05 United States AI NIAID NIH HHS; R21 AI092043-01 United States AI NIAID NIH HHS; R21 AI092043 United States AI NIAID NIH HHS; R21AI092043 United States AI NIAID NIH HHS; K02 AI085403 United States AI NIAID NIH HHS
    • الرقم المعرف:
      0 (Bacterial Proteins)
      0 (Guanine Nucleotide Exchange Factors)
      0 (SidD protein, Legionella pneumophila)
      0 (SidM protein, Legionella pneumophila)
      30KYC7MIAI (Aspartic Acid)
      EC 3.6.5.2 (rab1 GTP-Binding Proteins)
    • الموضوع:
      Date Created: 20110708 Date Completed: 20110803 Latest Revision: 20211020
    • الموضوع:
      20250114
    • الرقم المعرف:
      PMC3146296
    • الرقم المعرف:
      10.1038/nature10307
    • الرقم المعرف:
      21734656