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Structure and Activity of PPX/GppA Homologs from Escherichia coli and Helicobacter pylori

  1. Author:
    Song, He
    Dharmasena, Madushini N
    Wang, Chao
    Shaw,Gary
    Cherry,Scott
    Tropea,Joseph
    Jin,Ding
    Ji,Xinhua [ORCID]

  2. Author Address

    Macromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD, USA., RNA Biology Laboratory, National Cancer Institute, Frederick, MD, USA.,
    1. Year: 2020
    2. Date: May
    3. Epub Date: 2019 11 02
  2. Journal: The FEBS journal
    1. 287
    2. 9
    3. Pages: 1865-1885
  4. Type of Article: Article
  5. ISSN: 1742-464X
  1. Abstract:

    Rapid adaptation to environmental changes is crucial for bacterial survival. Almost all bacteria possess a conserved stringent response system to prompt transcriptional and metabolic responses toward stress. The adaptive process relies on alarmones, guanosine pentaphosphate (pppGpp) and tetraphosphate (ppGpp), to regulate global gene expression. The ppGpp is more potent than pppGpp in the regulatory activity and pppGpp phosphohydrolase (GppA) plays a key role in (p)ppGpp homeostasis. Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX), which mediates the metabolism of cellular inorganic polyphosphate. Here, our phylogenetic analysis of PPX/GppA homologs in bacteria shows a wide distribution with several distinct subfamilies, and our structural and functional analysis of Escherichia coli GppA and Helicobacter pylori PPX/GppA reveals unique properties of each homolog. These results explain how each homolog possesses its distinct functionality. © 2019 Federation of European Biochemical Societies.

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  1. Keywords:

External Sources

  1. View Full Text
  2. DOI: 10.1111/febs.15120
  3. PMID: 31679177
  4. View record in Web of Science®
  5. WOS: 000530101300012

Library Notes

  1. Fiscal Year: FY2019-2020
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