Cleavage of a tail-anchored protein by signal peptidase.
Tail-anchored proteins are post-translationally targeted and inserted into the endoplasmic reticulum membrane. They do not use the co-translational signal-recognition particle (SRP)-dependent pathway, but rather utilize an ill-defined, ATP-dependent mechanism. Here, we show that a tail-anchored protein can be cleaved by signal peptidase and that the sequence requirements for efficient cleavage seem to be the same as for cleavage of co-translationally targeted SRP-dependent proteins.
Nilsson
IngMarie
I
Department of Biochemistry and Biophysics, Stockholm University, SE-106 91, Stockholm, Sweden.
Johnson
Arthur E
AE
von Heijne
Gunnar
G
D000595:Amino Acid Sequence; D000818:Animals; D004285:Dogs; D004721:Endoplasmic Reticulum / Q000378:metabolism; D066298:In Vitro Techniques; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008861:Microsomes / Q000378:metabolism; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011499:Protein Processing, Post-Translational; D050683:R-SNARE Proteins; D011817:Rabbits; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012697:Serine Endopeptidases / Q000378:metabolism*
D008565:Membrane Proteins; D050683:R-SNARE Proteins; D011994:Recombinant Proteins; D012697:Serine Endopeptidases; C026515:type I signal peptidase