Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The catalytic mechanism of endoplasmic reticulum signal peptidase appears to be distinct from most eubacterial signal peptidases.
-
Active-site mutagenesis showed that Sec11 supplies residues needed for yeast ER signal peptidase activity.
"Instead, a serine, histidine, and two aspartic acids are important for signal peptidase activity by the Sec11p subunit of the yeast signal peptidase complex."
Signal peptidase and oligosaccharyltransferase interact in a sequential and dependent manner within the endoplasmic reticulum.
-
The signal peptides of prepro-alpha-factor and preinvertase must be removed in the yeast ER before nearby N-glycosylation sites are efficiently used.
"We demonstrate that the signal peptides of prepro-alpha-factor and preinvertase must be cleaved before Asn-X-Ser/Thr acceptor tripeptides located near the signal peptides of these precursors can be efficiently glycosylated within the endoplasmic reticulum of the yeast Saccharomyces cerevisiae."
Large-scale identification of yeast integral membrane protein interactions.
-
The study used modified split-ubiquitin screening to map interactions among S. cerevisiae integral membrane proteins.
"We carried out a large-scale screen to identify interactions between integral membrane proteins of Saccharomyces cerevisiae by using a modified split-ubiquitin technique."
Yeast signal peptidase contains a glycoprotein and the Sec11 gene product.
-
Purified yeast microsomal signal peptidase is a membrane complex that contains Sec11 as its 18-kDa chain.
"Partially purified yeast microsomal signal peptidase appears to be a complex of four polypeptides of 13, 18, 20, and 25 kDa. The 18-kDa chain is the product of the Sec11 gene, which is necessary for signal peptidase activity."
Solubilization and characterization of yeast signal peptidase.
-
Yeast signal peptidase is an integral membrane enzyme that removes the signal peptide from prepro-alpha-factor in vitro.
"Radiosequencing of the cleaved substrate revealed that the enzyme removed the signal peptide."
-
Yeast signal peptidase resists carbonate extraction, consistent with integral membrane association.
"The membrane association of yeast signal peptidase is resistant to carbonate extraction, indicating that it is an integral membrane protein."
SEC11 is required for signal peptide processing and yeast cell growth.
-
Temperature-sensitive sec11 mutant cells accumulate core-glycosylated invertase and acid phosphatase precursors that retain their signal peptides.
"At 37 degrees C, the restrictive growth temperature, sec11 cells accumulate core-glycosylated forms of invertase and acid phosphatase, each retaining an intact signal peptide."
-
Genetic analysis showed that SEC11 is authentic and essential.
"Genetic analysis indicates that the complementing clone contains the authentic SEC11 gene, and that a null mutation at the SEC11 locus is lethal."
The social and structural architecture of the yeast protein interactome.
-
The study mapped S. cerevisiae protein interactions using GFP-tagged affinity enrichment and two-dimensional AP-MS analysis.
"Here we develop a sensitive high-throughput method using highly reproducible affinity enrichment coupled to mass spectrometry combined with a quantitative two-dimensional analysis strategy to comprehensively map the interactome of Saccharomyces cerevisiae."
Structurally related Spc1p and Spc2p of yeast signal peptidase complex are functionally distinct.
-
Spc1 and Spc2 are noncatalytic yeast SPC subunits with distinct functions.
"These results indicate that although both Spc1p and Spc2p are noncatalytic, they are functionally distinct."
The yeast SPC22/23 homolog Spc3p is essential for signal peptidase activity.
-
Spc3 is the fourth subunit of yeast SPC and is essential for signal peptidase activity.
"Depletion of SPC3 leads to accumulation of precursors of secretory proteins in vivo and to the loss of the signal peptidase activity in vitro."
Spc2 modulates substrate- and cleavage site-selection in the yeast signal peptidase complex.
-
Loss or mutation of Spc2 compromises yeast SPC substrate discrimination and cleavage-site choice.
"Our data show that discrimination between substrates and identification of the cleavage site by SPC is compromised when Spc2 is absent or mutated."
The Sec11 C-terminal short helix promotes productive engagement of internal signal sequences with the signal peptidase complex.
-
The Sec11 C-terminal short helix spans the ER membrane and helps stabilize internal signal sequences during productive SPC engagement.
"While N-terminal signal sequences of varying hydrophobicity were efficiently cleaved, internal signal sequences with extended N-terminal region were selectively defective in cleavage in the absence of the Sec11 CTS."
-
Removing the Sec11 CTS does not abolish core Sec11-Spc3 assembly or cleavage of standard N-terminal signal sequences.
"Collectively, our data suggest that truncation of the Sec11 CTS neither destabilizes the SPC catalytic core nor compromises its proteolytic activity."