Lactococcus lactis: Recent Developments in Functional Expression of Membrane Proteins

2014 ◽  
pp. 107-132 ◽  
Author(s):  
Sana Bakari ◽  
François André ◽  
Daphné Seigneurin-Berny ◽  
Marcel Delaforge ◽  
Norbert Rolland ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Lactococcus Lactis ◽  
Functional Expression ◽  
Recent Developments

Functional Expression of Plant Membrane Proteins in Lactococcus lactis

2014 ◽  
pp. 147-165 ◽  
Author(s):  
Sylvain Boutigny ◽  
Emeline Sautron ◽  
Annie Frelet-Barrand ◽  
Lucas Moyet ◽  
Daniel Salvi ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Lactococcus Lactis ◽  
Functional Expression

Identification and Functional Expression of the Mitochondrial Pyruvate Carrier

Science ◽  
2012 ◽  
Vol 337 (6090) ◽  
pp. 93-96 ◽  
Author(s):  
Sébastien Herzig ◽  
Etienne Raemy ◽  
Sylvie Montessuit ◽  
Jean-Luc Veuthey ◽  
Nicola Zamboni ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Lactococcus Lactis ◽  
Mitochondrial Membrane ◽  
Functional Expression ◽  
Inner Mitochondrial Membrane ◽  
Molecular Identity ◽  
Mitochondrial Pyruvate Carrier ◽  
Essential Components ◽  
Yeast Mutants

The transport of pyruvate, the end product of glycolysis, into mitochondria is an essential process that provides the organelle with a major oxidative fuel. Although the existence of a specific mitochondrial pyruvate carrier (MPC) has been anticipated, its molecular identity remained unknown. We report that MPC is a heterocomplex formed by two members of a family of previously uncharacterized membrane proteins that are conserved from yeast to mammals. Members of the MPC family were found in the inner mitochondrial membrane, and yeast mutants lacking MPC proteins showed severe defects in mitochondrial pyruvate uptake. Coexpression of mouse MPC1 and MPC2 in Lactococcus lactis promoted transport of pyruvate across the membrane. These observations firmly establish these proteins as essential components of the MPC.

scholarly journals Lactococcus lactis, an Alternative System for Functional Expression of Peripheral and Intrinsic Arabidopsis Membrane Proteins

PLoS ONE ◽  
2010 ◽  
Vol 5 (1) ◽  
pp. e8746 ◽  
Author(s):  
Annie Frelet-Barrand ◽  
Sylvain Boutigny ◽  
Lucas Moyet ◽  
Aurélien Deniaud ◽  
Daphné Seigneurin-Berny ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Lactococcus Lactis ◽  
Functional Expression ◽  
Alternative System

Functional expression of mouse insulin-like growth factor-I with food-grade vector in Lactococcus lactis NZ9000

2012 ◽  
Vol 54 (5) ◽  
pp. 404-409 ◽  
Author(s):  
G. Gao ◽  
J.-J. Qiao ◽  
C.-H. Yang ◽  
D.-Z. Jiang ◽  
R.-Q. Li ◽  
...  
Keyword(s):  
Growth Factor ◽  
Lactococcus Lactis ◽  
Functional Expression ◽  
Insulin Like Growth Factor ◽  
Food Grade ◽  
Factor I ◽  
Growth Factor I

Evolved Lactococcus lactis Strains for Enhanced Expression of Recombinant Membrane Proteins

2010 ◽  
Vol 401 (1) ◽  
pp. 45-55 ◽  
Author(s):  
Daniel M. Linares ◽  
Eric R. Geertsma ◽  
Bert Poolman
Keyword(s):  
Membrane Proteins ◽  
Lactococcus Lactis ◽  
Enhanced Expression

Evolved Escherichia coli Strains for Amplified, Functional Expression of Membrane Proteins

2014 ◽  
Vol 426 (1) ◽  
pp. 136-149 ◽  
Author(s):  
Nadia Gul ◽  
Daniel M. Linares ◽  
Franz Y. Ho ◽  
Bert Poolman
Keyword(s):  
Escherichia Coli ◽  
Membrane Proteins ◽  
Functional Expression

Recent advances in the electrochemistry and spectroelectrochemistry of membrane proteins

2013 ◽  
Vol 394 (5) ◽  
pp. 593-609 ◽  
Author(s):  
Frederic Melin ◽  
Petra Hellwig
Keyword(s):  
Membrane Proteins ◽  
Redox Reactions ◽  
Pathogenic Bacteria ◽  
Alternative Methods ◽  
Natural Processes ◽  
Surface Enhanced ◽  
Recent Developments ◽  
Specific Membrane ◽  
Photosynthesis And Respiration

Abstract Integral membrane proteins are encountered in fundamental natural processes, such as photosynthesis and respiration. The relation between the structure of the proteins and their function and dynamics are still not clear in most cases. Once fully understood, these processes could ultimately help researchers to develop alternative methods for producing energy, either from light or biomass. They could also lead to more efficient antibiotics, which would selectively inhibit a specific membrane protein of pathogenic bacteria. Since the chemical reactions involved in both photosynthesis and respiration are redox reactions, electrochemical methods can play a considerable role in uncovering their mechanisms. The electrochemical characterization of membrane proteins is, however, quite challenging. An overview on the techniques used for the characterization of membrane proteins, including classical approaches such as voltammetry and spectroelectrochemistry, and recent developments, such as their combination with surface-enhanced techniques is given.

scholarly journals Methods for the solubilisation of membrane proteins: the micelle-aneous world of membrane protein solubilisation

2021 ◽  
Author(s):  
Giedre Ratkeviciute ◽  
Benjamin F. Cooper ◽  
Timothy J. Knowles
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Protein Stability ◽  
Lipid Membranes ◽  
Lipid Membrane ◽  
Modus Operandi ◽  
Membrane Mimetic ◽  
Aqueous Environments ◽  
Recent Developments

The solubilisation of membrane proteins (MPs) necessitates the overlap of two contradictory events; the extraction of MPs from their native lipid membranes and their subsequent stabilisation in aqueous environments. Whilst the current myriad of membrane mimetic systems provide a range of modus operandi, there are no golden rules for selecting the optimal pipeline for solubilisation of a specific MP hence a miscellaneous approach must be employed balancing both solubilisation efficiency and protein stability. In recent years, numerous diverse lipid membrane mimetic systems have been developed, expanding the pool of available solubilisation strategies. This review provides an overview of recent developments in the membrane mimetic field, with particular emphasis placed upon detergents, polymer-based nanodiscs and amphipols, highlighting the latest reagents to enter the toolbox of MP research.

scholarly journals Dynamic Nuclear Polarization of Biomembrane Assemblies

Biomolecules ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 1246
Author(s):  
Nhi T. Tran ◽  
Frédéric Mentink-Vigier ◽  
Joanna R. Long
Keyword(s):  
Membrane Proteins ◽  
Dynamic Nuclear Polarization ◽  
Nuclear Polarization ◽  
Atomic Scale ◽  
Nuclear Spins ◽  
Nmr Studies ◽  
Nmr Characterization ◽  
Recent Developments ◽  
Lipid Assemblies

While atomic scale structural and dynamic information are hallmarks of nuclear magnetic resonance (NMR) methodologies, sensitivity is a fundamental limitation in NMR studies. Fully exploiting NMR capabilities to study membrane proteins is further hampered by their dilution within biological membranes. Recent developments in dynamic nuclear polarization (DNP), which can transfer the relatively high polarization of unpaired electrons to nuclear spins, show promise for overcoming the sensitivity bottleneck and enabling NMR characterization of membrane proteins under native-like conditions. Here we discuss fundamental aspects of DNP-enhanced solid-state NMR spectroscopy, experimental details relevant to the study of lipid assemblies and incorporated proteins, and sensitivity gains which can be realized in biomembrane-based samples. We also present unique insights which can be gained from DNP measurements and prospects for further development of the technique for elucidating structures and orientations of membrane proteins in native lipid environments.

Sign in / Sign up

Export Citation Format

Share Document