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Protein import into yeast mitochondria is inhibited by antibodies raised against 45‐kd proteins of the outer membrane.
Author(s) -
Ohba M.,
Schatz G.
Publication year - 1987
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1987.tb02477.x
Subject(s) - antiserum , biology , mitochondrion , bacterial outer membrane , trypsin , membrane protein , inner mitochondrial membrane , mitochondrial membrane transport protein , mitochondrial carrier , biochemistry , yeast , inner membrane , membrane , microbiology and biotechnology , antibody , enzyme , escherichia coli , gene , immunology
Import of several precursor proteins into isolated yeast mitochondria is inhibited by rabbit antiserum raised against the total mitochondrial outer membrane or against electrophoretically purified 45‐kd outer membrane proteins. Antisera against other outer membrane proteins are only marginally active or inactive. Inhibition by the antiserum against 45‐kd proteins is only weak with untreated mitochondria, but reaches 80‐90% with mitochondria that had been pretreated with 0.1 mg/ml trypsin. This trypsin pretreatment by itself inhibits precursor import only slightly (30‐50%). Selective inhibition of import does not correlate with binding of the various IgGs to the mitochondrial surface and is also observed with the corresponding Fab fragments. Inhibition by antibodies against 45‐kd outer membrane proteins strongly suggests the existence of a mitochondrial surface protein mediating protein import and offers a means of isolating this protein.