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. 1987 May;169(5):1794–1800. doi: 10.1128/jb.169.5.1794-1800.1987

Suppression of a signal sequence mutation by an amino acid substitution in the mature portion of the maltose-binding protein.

W H Cover, J P Ryan, P J Bassford Jr, K A Walsh, J Bollinger, L L Randall
PMCID: PMC212026  PMID: 3553148

Abstract

An unusual spontaneous pseudorevertant of an Escherichia coli strain carrying the signal sequence point mutation malE14-1 was characterized. The suppressor mutation, malE2261, resulted in a single substitution of an aspartyl residue for a tyrosyl residue at position 283 in the sequence of the mature maltose-binding protein. The precursor retained the malE14-1 point mutation in the signal sequence. The pseudorevertant carrying both malE14-1 and malE2261 exported twice the amount of maltose-binding protein as that of the mutant carrying the malE14-1 allele alone but only 18% of the amount exported by a strain producing wild-type maltose-binding protein. A strain carrying the suppressor allele malE2261 in combination with a wild-type signal sequence exported normal quantities of maltose-binding protein to the periplasm. Mature MalE2261 had a Kd for maltose of 27 microM, compared with 3.6 microM for mature wild-type maltose-binding protein. The precursor species than contained both changes resulting from malE14-1 and malE2261 was significantly less stable in the cytoplasm than was the precursor containing only the change encoded by malE14-1.

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Selected References

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