ArticleEuropean biophysics journal : EBJ2015
MscCG from Corynebacterium glutamicum: functional significance of the C-terminal domain.
Article in European biophysics journal : EBJ, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- The diverse gating mechanisms of bacterial MscS-like ion channels.Biochemical Society transactions · 2026Review
- The MscS channel frombioRxiv : the preprint server for biology · 2026Article
- Harnessing the thermotolerant methylotroph Bacillus methanolicus for methanol-based synthetic L-proline production.Microbial cell factories · 2026Article
- "Force-From-Lipids" Dependence of the MscCG Mechanosensitive Channel Gating on Anionic Membranes.Microorganisms · 2023Article
- Induction of glutamic acid production by copper in Corynebacterium glutamicum.Applied microbiology and biotechnology · 2021Article
- Review
- Corynebacterium glutamicum mechanosensitive channels: towards unpuzzling "glutamate efflux" for amino acid production.Biophysical reviews · 2018Review
- Evolutionary specialization of MscCG, an MscS-like mechanosensitive channel, in amino acid transport in Corynebacterium glutamicum.Scientific reports · 2018Article
- A Novel Corynebacterium glutamicum l-Glutamate Exporter.Applied and environmental microbiology · 2018Article
- Biophysics of Mechanotransduction.European biophysics journal : EBJ · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Corynebacterium glutamicum is used in microbial biotechnology for the production of amino acids, e.g., glutamate and lysine. Excretion of glutamate into the surrounding medium under production conditions is mediated by MscCG, an MscS-type mechanosensitive channel. In difference to most other MscS-type channel proteins, MscCG carries, in addition to the N-terminal pore domain, a long C-terminal domain that amounts to about half of the size of the protein and harbors an additional transmembrane segment. Here we study the impact of the C-terminal domain on both functions of MscCG as mechanosensitive channel and as glutamate exporter. Sequential truncations of the C-terminal domain were applied, as well as deletion of particular subdomains, replacement of these segments by other amino acid sequences, and sequence randomization. Several parameters of cell physiology and bioenergetics of the obtained mutants related to both glutamate excretion and response to osmotic stress were quantified. All three subdomains of the C-terminal domain, i.e., the periplasmic loop, the fourth transmembrane segment, and the cytoplasmic loop, proved to be of core significance for MscCG function, in particular for glutamate excretion.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.