AspC-mediated aspartate metabolism coordinates the Escherichia coli cell cycle

PLoS One. 2014 Mar 26;9(3):e92229. doi: 10.1371/journal.pone.0092229. eCollection 2014.

Abstract

Background: The fast-growing bacterial cell cycle consists of at least two independent cycles of chromosome replication and cell division. To ensure proper cell cycles and viability, chromosome replication and cell division must be coordinated. It has been suggested that metabolism could affect the Escherichia coli cell cycle, but the idea is still lacking solid evidences.

Methodology/principle findings: We found that absence of AspC, an aminotransferase that catalyzes synthesis of aspartate, led to generation of small cells with less origins and slow growth. In contrast, excess AspC was found to exert the opposite effect. Further analysis showed that AspC-mediated aspartate metabolism had a specific effect in the cell cycle, as only extra aspartate of the 20 amino acids triggered production of bigger cells with more origins per cell and faster growth. The amount of DnaA protein per cell was found to be changed in response to the availability of AspC. Depletion of (p)ppGpp by ΔrelAΔspoT led to a slight delay in initiation of replication, but did not change the replication pattern found in the ΔaspC mutant.

Conclusion/significances: The results suggest that AspC-mediated metabolism of aspartate coordinates the E. coli cell cycle through altering the amount of the initiator protein DnaA per cell and the division signal UDP-glucose. Furthermore, AspC sequence conservation suggests similar functions in other organisms.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspartic Acid / metabolism*
  • Bacterial Proteins / metabolism
  • Cell Cycle*
  • Conserved Sequence
  • DNA Replication
  • DNA-Binding Proteins / metabolism
  • Escherichia coli / cytology*
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Escherichia coli / growth & development
  • Gene Deletion
  • Genes, Bacterial
  • Guanosine Tetraphosphate / metabolism
  • Models, Biological
  • Molecular Sequence Data
  • Phenotype
  • Replication Origin
  • Transaminases / metabolism*

Substances

  • Bacterial Proteins
  • DNA-Binding Proteins
  • DnaA protein, Bacteria
  • Aspartic Acid
  • Guanosine Tetraphosphate
  • Transaminases

Grants and funding

The work was supported by grants from the National Natural Science Foundation of China “NSFC”(Grant no. 31060015 to Morigen), the Natural Science Foundation of Inner Mongolia (Grant no. 2010Zd14 and 20102009 to Morigen), and the Program of Higher-level Talents of Inner Mongolia University “SPH-IMU” (Grant no. Z20090107 to Morigen). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.