Nitrogen storage regulation by PII protein: lessons learned from taxonomic outliers

FEBS J. 2020 Feb;287(3):439-442. doi: 10.1111/febs.15189. Epub 2020 Jan 13.

Abstract

The paper 'Interaction of N-acetyl-l-glutamate kinase with the PII signal transducer in the non-photosynthetic alga Polytomella parva: Co-evolution towards a hetero-oligomeric enzyme' by Selim et al. highlights how the study of a true taxonomic oddity, the heterotrophic unicellular alga P. parva, has been instrumental in uncovering the large potential for adaptive variation in the signaling complex of PII with the enzyme N-acetylglutamate kinase (NAGK). This complex modifies the regulatory properties of NAGK, allowing nitrogen stockpiling as arginine. In P. parva, a stable PII-NAGK complex is formed which lacks regulation by canonical PII effectors but which exhibits novel adaptive responses to nitrogen abundance mediated by glutamine, a neo-effector of PII proteins of photosynthetic eukaryotes.

Keywords: Polytomella parva; N-acetylglutamate kinase; algae (unicellular); arginine synthesis regulation; nitrogen assimilation; signaling.

Publication types

  • Research Support, Non-U.S. Gov't
  • Comment

MeSH terms

  • Bacterial Proteins
  • Humans
  • Nitrogen*
  • PII Nitrogen Regulatory Proteins
  • Phosphotransferases (Carboxyl Group Acceptor)*
  • Photosynthesis

Substances

  • Bacterial Proteins
  • PII Nitrogen Regulatory Proteins
  • Phosphotransferases (Carboxyl Group Acceptor)
  • acetylglutamate kinase
  • Nitrogen