The homologue of mammalian SPC12 is important for efficient signal peptidase activity in saccharomyces cerevisiae

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Item Type:	Article
Title:	The homologue of mammalian SPC12 is important for efficient signal peptidase activity in saccharomyces cerevisiae
Creators Name:	Fang, H., Panzner, S., Mullins, C., Hartmann, E. and Green, N.
Abstract:	The multisubunit signal peptidase catalyzes the cleavage of signal peptides and the degradation of some membrane proteins within the endoplasmic reticulum (ER). The only subunit of this enzyme functionally examined to date, yeast Sec11p, is related to signal peptidase I from bacteria. Since bacterial signal peptidase is capable of processing both prokaryotic and eukaryotic signal sequences as a monomer, it is unclear why the analogous enzyme in the ER contains proteins unrelated to signal peptidase I. To address this issue, the gene encoding Spc1p, the yeast homologue to mammalian SPC12, is isolated from the yeast Saccharomyces cerevisiae. Spc1p co-purifies and genetically interacts with Sec11p, but unlike Sec11p, Spc1p is not required for cell growth or the proteolytic processing of tested proteins in yeast. This indicates that only a subset of the ER signal peptidase subunits is required for signal peptidase and protein degradation activities in vivo. Through both genetic and biochemical criteria, Spc1p appears, however, to be important for efficient signal peptidase activity.
Keywords:	Amino Acid Sequence, Amino Acid Sequence Homology, Base Sequence, Frameshift Mutation, Fungal Proteins, Hydrolysis, Membrane Proteins, Molecular Sequence Data, Peptide Hydrolases, Phenotype, Protein Sorting Signals, Saccharomyces Cerevisiae, Saccharomyces Cerevisiae Proteins, Serine Endopeptidases, Animals, Dogs
Source:	Journal of Biological Chemistry
ISSN:	0021-9258
Publisher:	American Society for Biochemistry and Molecular Biology
Volume:	271
Number:	28
Page Range:	16460-16465
Date:	12 July 1996
Official Publication:	https://doi.org/10.1074/jbc.271.28.16460
PubMed:	View item in PubMed

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