論文

査読有り
2018年7月1日

LotA, a Legionella deubiquitinase, has dual catalytic activity and contributes to intracellular growth

Cellular Microbiology
  • Tomoko Kubori
  • ,
  • Tomoe Kitao
  • ,
  • Hiroki Ando
  • ,
  • Hiroki Nagai

20
7
開始ページ
e12840
終了ページ
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1111/cmi.12840
出版者・発行元
Blackwell Publishing Ltd

The intracellular bacterial pathogen, Legionella pneumophila, establishes the replicative niche as a result of the actions of a large array of effector proteins delivered via the Legionella Type 4 secretion system. Many effector proteins are expected to be involved in biogenesis and regulation of the Legionella-containing vacuole (LCV) that is highly decorated with ubiquitin. Here, we identified a Legionella deubiquitinase, designated LotA, by carrying out a genome analysis to find proteins resembling the eukaryotic ovarian tumour superfamily of cysteine proteases. LotA exhibits a dual ability to cleave ubiquitin chains that is dependent on 2 distinctive catalytic cysteine residues in the eukaryotic ovarian tumour domains. One cysteine dominantly contributes to the removal of ubiquitin from the LCVs by its polyubiquitin cleavage activity. The other specifically cleaves conjugated Lys6-linked ubiquitin. After delivered by the Type 4 secretion system, LotA localises on the LCVs via its PI(3)P-binding domain. The lipid-binding ability of LotA is crucial for ubiquitin removal from the vacuoles. We further analysed the functional interaction of the protein with the recently reported noncanonical ubiquitin ligases of L. pneumophila, revealing that the effector proteins are involved in coordinated regulation that contributes to bacterial growth in the host cells.

リンク情報
DOI
https://doi.org/10.1111/cmi.12840
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/29543380

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