Section 73
Chapter 72,175

Mutations which alter the function of the signal sequence of the maltose binding protein of Escherichia coli

Bedouelle, H.; Bassford, P.J.; Fowler, A.V.; Zabin, I.; Beckwith, J.; Hofnung, M.

Nature 285(5760): 78-81


ISSN/ISBN: 0028-0836
PMID: 6990274
DOI: 10.1038/285078a0
Accession: 072174600

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The maltose binding protein of Escherichia coli is secreted into the external periplasmic compartment of the cell by virtue of an amino-terminal signal sequence. Using DNA sequencing, we have determined the precise nature of mutations in the signal sequence which prevent the export of the maltose binding protein, causing it to accumulate in the cytoplasm in its precursor form. In most cases, the change of a single hydrophobic or uncharged amino acid to a charged amino acid within the signal sequence is sufficient to block the secretion process.

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