Elimination of the disulphide bond alters the conformation of mature lipo-β-lactamase in yeast

O. Pines*, O. Shani

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

When expressed in Saccharomyces cerevisiae the precursor of the hybrid prokaryotic protein lipo-β-lactamase is accumulated in reduced form whereas the majority of the mature form contains an intra molecular disulphide bond (oxidized form). We have previously shown that mature mutant lipo-β-lactamases in which the cysteine residue 131 was changed to either tyrosine or threonine lack the capacity to form a disulphide bond but are nevertheless processed and secreted efficiently in yeast. Here we show that these mutant mature lipo-β-lactamases, in yeast cell extracts, exhibit a tenfold lower β-lactamase-specific activity than the wild-type protein and that the mature mutant proteins are more susceptible to trypsin digestion. Thus, elimination of the disulphide bond alters the conformation of mature lipo-β-lactamase in yeast.

Original languageAmerican English
Pages (from-to)67-69
Number of pages3
JournalApplied Microbiology and Biotechnology
Volume38
Issue number1
DOIs
StatePublished - Oct 1992

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