Abstract
We present an approach that allows rapid determination of the topology of Escherichia coli inner-membrane proteins by a combination of topology prediction and limited fusion-protein analysis. We derive new topology models for 12 inner-membrane proteins: MarC, PstA, TatC, YaeL, YcbM, YddQ, YdgE, YedZ, YgjV, YiaB, YigG, and YnfA. We estimate that our approach should make it possible to arrive at highly reliable topology models for roughly 10% of the approximately 800 inner-membrane proteins thought to exist in E. coli.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alkaline Phosphatase
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Bacterial Proteins / metabolism*
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Cyclin-Dependent Kinases / genetics
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Cyclin-Dependent Kinases / metabolism*
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Escherichia coli / metabolism*
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Escherichia coli Proteins
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Genes, Reporter
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Green Fluorescent Proteins
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Luminescent Proteins / genetics
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Luminescent Proteins / metabolism
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Membrane Proteins / metabolism*
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Time Factors
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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Luminescent Proteins
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Membrane Proteins
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Recombinant Fusion Proteins
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Green Fluorescent Proteins
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Cyclin-Dependent Kinases
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Alkaline Phosphatase
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phoA protein, E coli