Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-11-7
pubmed:abstractText
The maltose-binding protein (MBP) of Escherichia coli is the periplasmic receptor of the maltose transport system. Previous studies have identified amino acid substitutions in an alpha/beta loop of the structure of MBP that are critical for the in vivo folding. To probe genetically the structural role of this surface loop, we generated a library in which the corresponding codons 32 and 33 of malE were mutagenized. The maltose phenotype, which correlates with a biologically active structure of MBP in the periplasm, indicated a considerable variability in the loop residues compatible with a correct in vivo folding pathway of the protein. By the same genetic screens, we characterized loop-variant MBPs associated with a defective periplasmic folding pathway and aggregated into inclusion bodies. Heat-shock induction with production of misfolded loop variants was examined using both lon-lacZ and htrA-lacZ fusions. We found that the extent of formation of inclusion bodies in the periplasm of E. coli, from misfolded loop variant MBPs, correlated with the level of heat-shock response regulated by the alternate heat-shock sigma factor, sigma 24.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/ATP-Binding Cassette Transporters, http://linkedlifedata.com/resource/pubmed/chemical/ATP-Dependent Proteases, http://linkedlifedata.com/resource/pubmed/chemical/AraF protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DegP protease, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/LivK protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Lon protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/MalE protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Maltose-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Periplasmic Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Periplasmic Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protease La, http://linkedlifedata.com/resource/pubmed/chemical/RbsB protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/galactose-binding protein, http://linkedlifedata.com/resource/pubmed/chemical/histidine-binding protein, http://linkedlifedata.com/resource/pubmed/chemical/lysyl-arginyl-ornithine-binding..., http://linkedlifedata.com/resource/pubmed/chemical/maltose transport system, E coli, http://linkedlifedata.com/resource/pubmed/chemical/sbp protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/sulfate-binding protein, bacteria
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
262
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
140-50
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:8831785-ATP-Binding Cassette Transporters, pubmed-meshheading:8831785-ATP-Dependent Proteases, pubmed-meshheading:8831785-Amino Acid Sequence, pubmed-meshheading:8831785-Bacterial Proteins, pubmed-meshheading:8831785-Calcium-Binding Proteins, pubmed-meshheading:8831785-Carrier Proteins, pubmed-meshheading:8831785-Databases, Factual, pubmed-meshheading:8831785-Escherichia coli, pubmed-meshheading:8831785-Escherichia coli Proteins, pubmed-meshheading:8831785-Heat-Shock Proteins, pubmed-meshheading:8831785-Hot Temperature, pubmed-meshheading:8831785-Inclusion Bodies, pubmed-meshheading:8831785-Lac Operon, pubmed-meshheading:8831785-Maltose-Binding Proteins, pubmed-meshheading:8831785-Molecular Sequence Data, pubmed-meshheading:8831785-Monosaccharide Transport Proteins, pubmed-meshheading:8831785-Mutagenesis, Site-Directed, pubmed-meshheading:8831785-Periplasmic Binding Proteins, pubmed-meshheading:8831785-Periplasmic Proteins, pubmed-meshheading:8831785-Protease La, pubmed-meshheading:8831785-Protein Structure, Secondary, pubmed-meshheading:8831785-Protein Structure, Tertiary, pubmed-meshheading:8831785-Serine Endopeptidases, pubmed-meshheading:8831785-Structure-Activity Relationship
pubmed:year
1996
pubmed:articleTitle
Probing the structural role of an alpha beta loop of maltose-binding protein by mutagenesis: heat-shock induction by loop variants of the maltose-binding protein that form periplasmic inclusion bodies.
pubmed:affiliation
Départment des Biotechnologies, Institut Pasteur, Paris, France.
pubmed:publicationType
Journal Article