Determinants of Membrane Protein Topology

The topology of the integral membrane protein MalF, which is required for maltose transport in Escherichia coli, has been analyzed using fusions of alkaline phosphatase (EC 3.1.3.1). The properties of such fusion strains support a MalF structure previously proposed on theoretical grounds. Several tr...

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Bibliographic Details
Published inProceedings of the National Academy of Sciences - PNAS Vol. 84; no. 23; pp. 8525 - 8529
Main Authors Boyd, Dana, Manoil, Colin, Beckwith, Jon
Format Journal Article
LanguageEnglish
Published Washington, DC National Academy of Sciences of the United States of America 01.12.1987
National Acad Sciences
Subjects
Alkaline Phosphatase
Amino acids
ATP-Binding Cassette Transporters
Bacteriology
Biogenesis of cell structures, supramolecular organization
Biological and medical sciences
Carrier Proteins
Cytoplasm
DNA
DNA Mutational Analysis
Escherichia coli
Escherichia coli Proteins
Fundamental and applied biological sciences. Psychology
Maltose-Binding Proteins
Membrane Proteins
Microbiology
Monosaccharide Transport Proteins
P branes
Periplasm
Phosphatases
Plasmids
Protein Conformation
Proteins
Recombinant Fusion Proteins
Recombinant Proteins
Structure-Activity Relationship
Topology
Membrane protein
Escherichia coli
Topography
Plasma membrane
Bacteria
Maltose
Escherichieae
Carrier protein
Enterobacteriaceae
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Summary:The topology of the integral membrane protein MalF, which is required for maltose transport in Escherichia coli, has been analyzed using fusions of alkaline phosphatase (EC 3.1.3.1). The properties of such fusion strains support a MalF structure previously proposed on theoretical grounds. Several transmembrane segments within MalF can act as signal sequences in exporting alkaline phosphatase. Other transmembrane sequences, in conjunction with cytoplasmic domains, can stably anchor alkaline phosphatase in the cytoplasm. Our results suggest that features of the amino acid sequence (possibly the positively charged amino acids) of the cytoplasmic domains of membrane proteins are important in anchoring these domains in the cytoplasm. These studies in conjunction with our earlier results show that alkaline phosphatase fusions to membrane proteins can be an important aid in analyzing membrane topology and its determinants.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.84.23.8525