Linked Life Data

20099140

Source:http://linkedlifedata.com/resource/pubmed/id/20099140

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2010-1-25
pubmed:abstractText
Membrane proteins play key roles in cellular physiology, and they are important drug targets. Approximately 25% of all genes identified in sequenced genomes are known to encode membrane proteins; however, the majority have no assigned function. Although the resolution of soluble protein structure has entered the high-throughput stage, only 100 high-resolution structures of membrane proteins have been described until now. Lactococcus lactis is a gram-positive lactic bacterium that has been used traditionally in food fermentations, but it is now used widely in biotechnology for large-scale overproduction of heterologously expressed proteins. Various expression vectors based on either constitutive or inducible promoters exist. The nisin-inducible controlled gene expression (NICE) system is the most suitable for recombinant membrane protein expression allowing for fine control of gene expression based on the autoregulation mechanism of the bacteriocin nisin. Recombinant membrane proteins can be produced with affinity tags for efficient detection and purification from crude membrane protein extracts. The purpose of this chapter is to provide a detailed protocol for the expression of membrane proteins and their detection using the Strep-tag II affinity tag in L. lactis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1940-6029
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
601
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
67-85
pubmed:dateRevised
2010-4-19
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Membrane protein expression in Lactococcus lactis.
pubmed:affiliation
Laboratoire de Physiologie Cellulaire Végétale, CNRS (UMR-5168)/CEA/INRA (UMR-1200), Université Joseph Fourier, iRTSV, CEA-Grenoble, France. annie.barrand-frelet@cea.fr
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't