Abstract
We used the enzymes beta-lactamase and alkaline phosphatase to quantitatively evaluate the release of periplasmic proteins from E. coli cells transformed by plasmids harboring gene 3 of phage fd. Different deletion mutants of gene 3 released varying fractions of the enzymes. From these results we conclude that essentially the amino-terminal proximal part, upstream of the first glycine-rich region but not this region itself, is responsible for the excretion of periplasmic proteins in E. coli cells expressing the gene 3 protein of phage fd.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alkaline Phosphatase / metabolism
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Capsid Proteins
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Coliphages / genetics*
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DNA-Binding Proteins / biosynthesis
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DNA-Binding Proteins / genetics*
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Escherichia coli / enzymology
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Escherichia coli / genetics*
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Escherichia coli / growth & development
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Gene Expression
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Glycine / chemistry
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Mutation
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Plasmids
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Viral Envelope Proteins / genetics*
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Viral Fusion Proteins*
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Viral Proteins / biosynthesis
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Viral Proteins / chemistry
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Viral Proteins / genetics*
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beta-Lactamases / metabolism
Substances
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Capsid Proteins
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DNA replication complex protein, Bacteriophage lambda
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DNA-Binding Proteins
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Viral Envelope Proteins
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Viral Fusion Proteins
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Viral Proteins
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Alkaline Phosphatase
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beta-Lactamases
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Glycine