Analysis of protein condensation for enzymes involved in extracellular glutamate overproduction in Corynebacterium glutamicum

Clicks: 14
ID: 333695
2026
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal
Emerging

Ranked #87 of 97 articles by views in bioscience biotechnology and biochemistry

Most read Least read

Bar heights use a square-root scale.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Abstract
Abstract During extracellular glutamate overproduction in Corynebacterium glutamicum, an increase in metabolic flux toward glutamate synthesis occurs without an increase in the transcriptional or translational levels of relevant enzymes, suggesting the involvement of unprecedented post-translational regulatory mechanisms. Here, we investigated the relationship of enzyme condensation with the metabolic shifts that lead to glutamate overproduction. We systematically analyzed the subcellular localization of enzymes involved in glutamate overproduction using fluorescent protein tagging to identify enzyme condensates in C. glutamicum. Our analyses revealed punctate localization, suggesting condensate formation for glyceraldehyde 3-phosphate dehydrogenase, enolase, pyruvate carboxylase, citrate synthase, pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase (ODH) complexes, and the intrinsic ODH inhibitor OdhI. Notably, enolase frequently formed condensates under glutamate-producing conditions, without changes in protein abundance. Our findings provide key insights into the intracellular dynamics of central carbon metabolic enzymes and offer a novel perspective on the mechanisms underlying glutamate overproduction in C. glutamicum.
Reference Key
openalex_W7223377636 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Makoto Nagaoka, Kaito Ueda, Makoto Nishiyama, Saori Kosono
Journal bioscience biotechnology and biochemistry
Year 2026
DOI
10.1093/bbb/zbag160
URL
Keywords Keywords not found

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

No comments yet. Be the first to comment on this article.