Improved tolerance of recombinant Chlamydomonas rainhardtii with putative 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase from Pyropia yezoensis to nitrogen starvation

J Microbiol. 2022 Jan;60(1):63-69. doi: 10.1007/s12275-022-1491-7. Epub 2021 Dec 29.

Abstract

In a previous study, a putative 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase (ACMSD) was highly expressed in a mutant strain of Pyropia yezoensis, which exhibited an improved growth rate compared to its wild strain. To investigate the functional role of the putative ACMSD (Pyacmsd) of P. yezoensis, the putative Pyacmsd was cloned and expressed in Chlamydomonas reinhardtii. Recombinant C. reinhardtii cells with Pyacmsd (Cr_Pyacmsd) exhibited enhanced tolerance compared to control C. reinhardtii cells (Cr_control) under nitrogen starvation. Notably, Cr_Pyacmsd cells showed accumulation of lipids in nitrogen-enriched conditions. These results demonstrate the role of Pyacmsd in the generation of acetyl-coenzyme A. Thus, it can be used to enhance the production of biofuel using microalgae such as C. reinhardtii and increase the tolerance of other biological systems to nitrogen-deficient conditions.

Keywords: 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase; Chlamydomonas reinhardtii; Pyropia yezoensis; lipid accumulation; nitrogen starvation.

MeSH terms

  • Carboxy-Lyases / genetics*
  • Carboxy-Lyases / metabolism
  • Chlamydomonas reinhardtii / genetics*
  • Chlamydomonas reinhardtii / metabolism*
  • Cloning, Molecular
  • Gene Expression*
  • Nitrogen / metabolism*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Rhodophyta / enzymology*
  • Rhodophyta / genetics

Substances

  • Recombinant Proteins
  • Carboxy-Lyases
  • Nitrogen