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Disruption of the Lys‐290‐Glu‐342 salt bridge in human α 1 ‐antitrypsin does not prevent its synthesis and secretion
Author(s) -
Foreman R.C.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80760-3
Subject(s) - salt bridge , secretion , mutant , chemistry , complementary dna , xenopus , mutagenesis , biochemistry , lysine , site directed mutagenesis , microbiology and biotechnology , amino acid , biology , gene
The object of this work was to test the hypothesis that failure to secrete the Z variant of human α 1 ‐antitrypsin is related to the loss of a particular structural feature, the Lys‐290 to Glu‐342 salt bridge. Oligonucleotide‐directed mutagenesis was used to disrupt the salt bridge by substituting a glutamic acid for lysine at residue 290. RNA transcripts prepared from this mutant DNA and from the normal cDNA were both able to direct the synthesis of protein in a cell‐free system and after injection into Xenopus oocytes. Furthermore, the constructed mutant α‐antitrypsin was secreted as readily as the normal inhibitor.