Lactococcus lactis: Recent Developments in Functional Expression of Membrane Proteins

Author(s):  
Sana Bakari ◽  
François André ◽  
Daphné Seigneurin-Berny ◽  
Marcel Delaforge ◽  
Norbert Rolland ◽  
...  
Author(s):  
Sylvain Boutigny ◽  
Emeline Sautron ◽  
Annie Frelet-Barrand ◽  
Lucas Moyet ◽  
Daniel Salvi ◽  
...  

Science ◽  
2012 ◽  
Vol 337 (6090) ◽  
pp. 93-96 ◽  
Author(s):  
Sébastien Herzig ◽  
Etienne Raemy ◽  
Sylvie Montessuit ◽  
Jean-Luc Veuthey ◽  
Nicola Zamboni ◽  
...  

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.


PLoS ONE ◽  
2010 ◽  
Vol 5 (1) ◽  
pp. e8746 ◽  
Author(s):  
Annie Frelet-Barrand ◽  
Sylvain Boutigny ◽  
Lucas Moyet ◽  
Aurélien Deniaud ◽  
Daphné Seigneurin-Berny ◽  
...  

2010 ◽  
Vol 401 (1) ◽  
pp. 45-55 ◽  
Author(s):  
Daniel M. Linares ◽  
Eric R. Geertsma ◽  
Bert Poolman

2014 ◽  
Vol 426 (1) ◽  
pp. 136-149 ◽  
Author(s):  
Nadia Gul ◽  
Daniel M. Linares ◽  
Franz Y. Ho ◽  
Bert Poolman

2013 ◽  
Vol 394 (5) ◽  
pp. 593-609 ◽  
Author(s):  
Frederic Melin ◽  
Petra Hellwig

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.


Author(s):  
Giedre Ratkeviciute ◽  
Benjamin F. Cooper ◽  
Timothy J. Knowles

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.


Biomolecules ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 1246
Author(s):  
Nhi T. Tran ◽  
Frédéric Mentink-Vigier ◽  
Joanna R. Long

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.


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