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Mitochondrial presequences can induce aggregation of unfolded proteins
Author(s) -
Endo Toshiya,
Mitsui Satoko,
Roise David
Publication year - 1995
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(95)00015-2
Subject(s) - mitochondrion , cytosol , alpha lactalbumin , lactalbumin , chemistry , function (biology) , biophysics , microbiology and biotechnology , biochemistry , biology , enzyme
We have studied the interactions between various synthetic peptides and two model unfolded proteins, reduced α‐lactalbumin and reduced and carboxymethylated α‐lactalbumin. We found that mitochondrial presequences could induce aggregation of the unfolded α‐lactalbumins but not of the native α‐lactalbumin. The presequence‐induced aggregation of unfolded α‐lactalbumin was dependent on electrostatic interactions and on the amphiphilicity of the presequences. Since positive charge and amphiphilicity are necessary for the targeting function of mitochondrial presequences, presequence‐induced aggregation may be responsible for the instability of mitochondrial precursor proteins and may need to be inhibited by binding factors in the cytosol.