ArticlePloS one2011
The response of Lactococcus lactis to membrane protein production.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 45 citations in OpenAlex.
- Multiple novel membrane proteins involve phthalate ester degradation inApplied and environmental microbiology · 2026Article
- High-Resolution Chrono-Transcriptome of Lactococcus lactis Reveals That It Expresses Proteins with Adapted Size and pI upon Acidification and Nutrient Starvation.Applied and environmental microbiology · 2022Article
- New insights into the resistance mechanism for the BceAB-type transporter SaNsrFP.Scientific reports · 2022Article
- The Effect of Recombinant Protein Production inMicroorganisms · 2022Review
- Review
- Functional production of clostridial circularin A inFrontiers in microbiology · 2022Article
- Plasmid Replicons for the Production of Pharmaceutical-Grade pDNA, Proteins and Antigens byInternational journal of molecular sciences · 2021Review
- Cell wall homeostasis in lactic acid bacteria: threats and defences.FEMS microbiology reviews · 2020Review
- Constitutively-stressed yeast strains are high-yielding for recombinant Fps1: implications for the translational regulation of an aquaporin.Microbial cell factories · 2017Article
- Early Transcriptome Response ofFrontiers in microbiology · 2017Article
- On the Spatial Organization of mRNA, Plasmids, and Ribosomes in a Bacterial Host Overexpressing Membrane Proteins.PLoS genetics · 2016Article
- Stress Physiology of Lactic Acid Bacteria.Microbiology and molecular biology reviews : MMBR · 2016Review
- Lactococcus lactis is an Efficient Expression System for Mammalian Membrane Proteins Involved in Liver Detoxification, CYP3A4, and MGST1.Molecular biotechnology · 2016Article
- Factors Affecting Inducible Expression of Outer Membrane Protein A (OmpA) of Shigella dysenteriae Type-1 in Lactococcus lactis Using Nisin Inducible Controlled Expression (NICE).Indian journal of microbiology · 2016Article
- Systematic identification of tRNAome and its dynamics in Lactococcus lactis.Molecular microbiology · 2014Article
- Cell wall structure and function in lactic acid bacteria.Microbial cell factories · 2014Review
- Transcriptional regulation of fatty acid biosynthesis in Lactococcus lactis.Journal of bacteriology · 2013Article
- The maltose ABC transporter in Lactococcus lactis facilitates high-level sensitivity to the circular bacteriocin garvicin ML.Antimicrobial agents and chemotherapy · 2012Article
- Efficient overproduction of membrane proteins in Lactococcus lactis requires the cell envelope stress sensor/regulator couple CesSR.PloS one · 2011Article
- How to achieve high-level expression of microbial enzymes: strategies and perspectives.BioengineeredReview
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe biogenesis of membrane proteins is more complex than that of water-soluble proteins, and recombinant expression of membrane proteins in functional form and in amounts high enough for structural and functional studies is often problematic. To better engineer cells towards efficient protein production, we set out to understand and compare the cellular consequences of the overproduction of both classes of proteins in Lactococcus lactis, employing a combined proteomics and transcriptomics approach. METHODOLOGY AND
findingsHighly overproduced and poorly expressed membrane proteins both resulted in severe growth defects, whereas amplified levels of a soluble substrate receptor had no effect. In addition, membrane protein overproduction evoked a general stress response (upregulation of various chaperones and proteases), which is probably due to accumulation of misfolded protein. Notably, upon the expression of membrane proteins a cell envelope stress response, controlled by the two-component regulatory CesSR system, was observed.
conclusionsThe physiological response of L. lactis to the overproduction of several membrane proteins was determined and compared to that of a soluble protein, thus offering better understanding of the bottlenecks related to membrane protein production and valuable knowledge for subsequent strain engineering.
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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.