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Information on EC 2.4.1.370 - inositol phosphorylceramide mannosyltransferase
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2.4.1.370 inositol phosphorylceramide mannosyltransferaseIUBMB Comments
The simplest complex sphingolipid of yeast, inositol-phospho-alpha-hydroxyphytoceramide (IPC), is usually mannosylated to yield mannosyl-inositol-phospho-alpha hydroxyphytoceramide (MIPC). The enzyme is located in the Golgi apparatus, and utilizes GDP-mannose as the mannosyl group donor. It consists of a catalytic subunit (SUR1 or CSH1) and a regulatory subunit (CSG2).
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Word Map
- 2.4.1.370
-
mannosylation
- sphingolipids
-
ca2+-sensitive
- ipc
- albicans
-
multicopy
-
ca2+-induced
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
=
+
+
a very-long-chain inositol phospho-(2'R)-2'-hydroxyphytoceramide
=
a very-long-chain mannosylinositol phospho-(2'R)-2'-hydroxyphytoceramide
+
Synonyms
csh1p, csg1p, bcl21, ybr161w, inositol phosphorylceramide mannosyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BCL21
Csg1
Csg1p
CSH1
Csh1p
SUR1
YBR161w
CSH1
-
-
-
-
SUR1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GDP-alpha-D-mannose + a very-long-chain inositol phospho-(2'R)-2'-hydroxyphytoceramide = a very-long-chain mannosylinositol phospho-(2'R)-2'-hydroxyphytoceramide + GDP
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-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
GDP-alpha-D-mannose:inositol phospho-(2'R)-2'-hydroxyphytoceramide mannosyltransferase
The simplest complex sphingolipid of yeast, inositol-phospho-alpha-hydroxyphytoceramide (IPC), is usually mannosylated to yield mannosyl-inositol-phospho-alpha hydroxyphytoceramide (MIPC). The enzyme is located in the Golgi apparatus, and utilizes GDP-mannose as the mannosyl group donor. It consists of a catalytic subunit (SUR1 or CSH1) and a regulatory subunit (CSG2).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-alpha-D-mannose + a very-long-chain inositol phospho-(2'R)-2'-hydroxyphytoceramide
a very-long-chain mannosylinositol phospho-(2'R)-2'-hydroxyphytoceramide + GDP
GDP-alpha-D-mannose + a very-long-chain inositol phospho-(2'R)-2'-hydroxyphytoceramide
a very-long-chain mannosylinositol phospho-(2'R)-2'-hydroxyphytoceramide + GDP
-
-
-
?
GDP-alpha-D-mannose + a very-long-chain inositol phospho-(2'R)-2'-hydroxyphytoceramide
a very-long-chain mannosylinositol phospho-(2'R)-2'-hydroxyphytoceramide + GDP
-
-
-
?
GDP-alpha-D-mannose + a very-long-chain inositol phospho-(2'R)-2'-hydroxyphytoceramide
a very-long-chain mannosylinositol phospho-(2'R)-2'-hydroxyphytoceramide + GDP
-
-
-
?
GDP-alpha-D-mannose + a very-long-chain inositol phospho-(2'R)-2'-hydroxyphytoceramide
a very-long-chain mannosylinositol phospho-(2'R)-2'-hydroxyphytoceramide + GDP
-
-
-
?
additional information
?
-
substrate specificity, overview
-
-
-
additional information
?
-
substrate specificity, overview
-
-
-
additional information
?
-
substrate specificity, overview
-
-
-
additional information
?
-
substrate specificity, overview
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-alpha-D-mannose + a very-long-chain inositol phospho-(2'R)-2'-hydroxyphytoceramide
a very-long-chain mannosylinositol phospho-(2'R)-2'-hydroxyphytoceramide + GDP
GDP-alpha-D-mannose + a very-long-chain inositol phospho-(2'R)-2'-hydroxyphytoceramide
a very-long-chain mannosylinositol phospho-(2'R)-2'-hydroxyphytoceramide + GDP
-
-
-
?
GDP-alpha-D-mannose + a very-long-chain inositol phospho-(2'R)-2'-hydroxyphytoceramide
a very-long-chain mannosylinositol phospho-(2'R)-2'-hydroxyphytoceramide + GDP
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+ stimulates inositol phosphorylceramide (IPC) to mannosylinositol phosphorylceramide (MIPC) conversion, because of a Csg2-dependent increase in Csg1 levels
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Starvation
The CLS2 gene encodes a protein with multiple membrane-spanning domains that is important Ca2+ tolerance in yeast.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
integral membrane protein Csg1 exhibits a membrane topology with its C-terminus in the cytosol and its mannosyltransferase domain in the lumen
brenda
integral membrane protein Csh1 exhibits a membrane topology with its C-terminus in the cytosol and its mannosyltransferase domain in the lumen
brenda
-
integral membrane protein Csg1 exhibits a membrane topology with its C-terminus in the cytosol and its mannosyltransferase domain in the lumen
-
brenda
-
integral membrane protein Csh1 exhibits a membrane topology with its C-terminus in the cytosol and its mannosyltransferase domain in the lumen
-
brenda
additional information
complexed Csg1 functions in the Golgi and is then delivered to the vacuole for degradation
-
brenda
additional information
complexed Csg1 functions in the Golgi and is then delivered to the vacuole for degradation
-
brenda
additional information
uncomplexed Csh1 cannot exit from the endoplasmic reticulum. Complexed Csh1 functions in the Golgi and is then delivered to the vacuole for degradation
-
brenda
additional information
uncomplexed Csh1 cannot exit from the endoplasmic reticulum. Complexed Csh1 functions in the Golgi and is then delivered to the vacuole for degradation
-
brenda
additional information
-
complexed Csg1 functions in the Golgi and is then delivered to the vacuole for degradation
-
-
brenda
additional information
-
uncomplexed Csh1 cannot exit from the endoplasmic reticulum. Complexed Csh1 functions in the Golgi and is then delivered to the vacuole for degradation
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
deletion of the CSG2 gene reduces the Csg1p activity and abolishes the Csh1p activity. The DELTAcsg1/DELTAcsh1 double mutant is highly sensitive to Ca2+ and does not grow on the YPD plate medium
malfunction
deletion of the CSG2 gene reduces the Csg1p activity and abolishes the Csh1p activity. The DELTAcsg2 mutant, as well as the DELTAcsg1/DELTAcsh1 double mutant, is highly sensitive to Ca2+ and does not grow on the YPD plate medium
malfunction
DELTAcsg1 cells exhibit only a reduction in the synthesis of mannosylated sphingolipids compared with wild-type cells, whereas the DELTAcsg1/DELTAcsh1 double deletion mutant exhibits a total loss
malfunction
the SUR1/CSG1 gene is a dose-dependent suppressor of the Ca2+-sensitive phenotype of the csg2 mutant, but overexpression of CSG2 does not suppress the Ca2+-sensitivity of the csg1 mutant. The csg1 and csg2 mutants display normal growth in YPD, indicating that mannosylation of sphingolipids is not essential. Increased osmolarity of the growth medium increases the Ca2+ tolerance of csg1 and csg2 mutant cells, suggesting that altered cell wall synthesis causes Ca2+-induced death. Phenotypic characterization of csg1 mutants, overview. Cu2+ reverses the Ca2+ sensitivity of csg1 mutant cells
malfunction
-
deletion of the CSG2 gene reduces the Csg1p activity and abolishes the Csh1p activity. The DELTAcsg2 mutant, as well as the DELTAcsg1/DELTAcsh1 double mutant, is highly sensitive to Ca2+ and does not grow on the YPD plate medium
-
malfunction
-
DELTAcsg1 cells exhibit only a reduction in the synthesis of mannosylated sphingolipids compared with wild-type cells, whereas the DELTAcsg1/DELTAcsh1 double deletion mutant exhibits a total loss
-
malfunction
-
the SUR1/CSG1 gene is a dose-dependent suppressor of the Ca2+-sensitive phenotype of the csg2 mutant, but overexpression of CSG2 does not suppress the Ca2+-sensitivity of the csg1 mutant. The csg1 and csg2 mutants display normal growth in YPD, indicating that mannosylation of sphingolipids is not essential. Increased osmolarity of the growth medium increases the Ca2+ tolerance of csg1 and csg2 mutant cells, suggesting that altered cell wall synthesis causes Ca2+-induced death. Phenotypic characterization of csg1 mutants, overview. Cu2+ reverses the Ca2+ sensitivity of csg1 mutant cells
-
malfunction
-
deletion of the CSG2 gene reduces the Csg1p activity and abolishes the Csh1p activity. The DELTAcsg1/DELTAcsh1 double mutant is highly sensitive to Ca2+ and does not grow on the YPD plate medium
-
metabolism
sphingolipid metabolism and calcium sensitivity, overview
metabolism
-
sphingolipid metabolism and calcium sensitivity, overview
-
physiological function
complex sphingolipids in yeast are known to function in cellular adaptation to environmental changes. One of the yeast complex sphingolipids, mannosylinositol phosphorylceramide (MIPC), is produced by the redundant inositol phosphorylceramide (IPC) mannosyltransferases Csg1 and Csh1. The Ca2+-binding protein Csg2 can form a complex with either Csg1 or Csh1 and is considered to act as a regulatory subunit. After complexing with Csg2, both Csg1 and Csh1 function in the Golgi, and then are delivered to the vacuole for degradation. Csg2 has several regulatory functions for Csg1 and Csh1, including stability, transport, and gene expression. Differing effects of Csg2 on the degradation of isozymes Csg1 and Csh1 in the vacuole
physiological function
Csg1p and Csg2p are involved in the synthesis of mannosylinositol phosphorylceramide (MIPC) from inositol phosphorylceramide. Csg1p and Csh1p have redundant functions in MIPC synthesis. Csg2p interacts with both Csg1p and Csh1p. Two distinct inositol phosphorylceramide mannosyltransferase complexes, Csg1p-Csg2p and Csh1p-Csg2p, exist. Csg1p or Csh1p activity may be regulated by Ca2+ through Csg2p
physiological function
Csh1p is involved in the synthesis of mannosylinositol phosphorylceramide (MIPC) from inositol phosphorylceramide. Csg1p and Csh1p have redundant functions in MIPC synthesis. Csg2p interacts with both Csg1p and Csh1p. Two distinct inositol phosphorylceramide mannosyltransferase complexes, Csg1p-Csg2p and Csh1p-Csg2p, exist. Csg1p or Csh1p activity may be regulated by Ca2+ through Csg2p
physiological function
in the Golgi, IPC is mannosylated to form mannosylinositolphosphorylceramide (MIPC). Saccharomyces cerevisiae cells require two genes, CSG1/SUR1 and CSG2, for growth in 50 mM Ca2+, but not 50 mM Sr2+. CSG2 is previously shown to be required for the mannosylation of inositol-phosphorylceramide (IPC) to form mannosylinositol-phosphorylceramide (MIPC). SUR1/CSG1 is both genetically and biochemically related to CSG2. Like CSG2, SUR1/CSG1 is required for IPC mannosylation
physiological function
-
Csg1p and Csg2p are involved in the synthesis of mannosylinositol phosphorylceramide (MIPC) from inositol phosphorylceramide. Csg1p and Csh1p have redundant functions in MIPC synthesis. Csg2p interacts with both Csg1p and Csh1p. Two distinct inositol phosphorylceramide mannosyltransferase complexes, Csg1p-Csg2p and Csh1p-Csg2p, exist. Csg1p or Csh1p activity may be regulated by Ca2+ through Csg2p
-
physiological function
-
complex sphingolipids in yeast are known to function in cellular adaptation to environmental changes. One of the yeast complex sphingolipids, mannosylinositol phosphorylceramide (MIPC), is produced by the redundant inositol phosphorylceramide (IPC) mannosyltransferases Csg1 and Csh1. The Ca2+-binding protein Csg2 can form a complex with either Csg1 or Csh1 and is considered to act as a regulatory subunit. After complexing with Csg2, both Csg1 and Csh1 function in the Golgi, and then are delivered to the vacuole for degradation. Csg2 has several regulatory functions for Csg1 and Csh1, including stability, transport, and gene expression. Differing effects of Csg2 on the degradation of isozymes Csg1 and Csh1 in the vacuole
-
physiological function
-
in the Golgi, IPC is mannosylated to form mannosylinositolphosphorylceramide (MIPC). Saccharomyces cerevisiae cells require two genes, CSG1/SUR1 and CSG2, for growth in 50 mM Ca2+, but not 50 mM Sr2+. CSG2 is previously shown to be required for the mannosylation of inositol-phosphorylceramide (IPC) to form mannosylinositol-phosphorylceramide (MIPC). SUR1/CSG1 is both genetically and biochemically related to CSG2. Like CSG2, SUR1/CSG1 is required for IPC mannosylation
-
physiological function
-
Csh1p is involved in the synthesis of mannosylinositol phosphorylceramide (MIPC) from inositol phosphorylceramide. Csg1p and Csh1p have redundant functions in MIPC synthesis. Csg2p interacts with both Csg1p and Csh1p. Two distinct inositol phosphorylceramide mannosyltransferase complexes, Csg1p-Csg2p and Csh1p-Csg2p, exist. Csg1p or Csh1p activity may be regulated by Ca2+ through Csg2p
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SUR1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
382
3
44808
Swiss-Prot
Secretory Pathway (Reliability: 1)
CSH1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
376
3
44382
Swiss-Prot
Secretory Pathway (Reliability: 1)
A0A6J8CNQ2_MYTCO
551
1
65333
TrEMBL
Secretory Pathway (Reliability: 3)
A0A6J8D5C7_MYTCO
317
2
36847
TrEMBL
Secretory Pathway (Reliability: 1)
A0A812ES66_SEPPH
272
0
31578
TrEMBL
other Location (Reliability: 3)
A0A6J8EZP4_MYTCO
862
1
99505
TrEMBL
Secretory Pathway (Reliability: 2)
A0A6J8BN08_MYTCO
317
2
36706
TrEMBL
Secretory Pathway (Reliability: 2)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 47000, about, recombinant FLAG3-tagged enzyme, sequence calculation, x * 48000, glycosylated recombinant FLAG3-tagged enzyme, SDS-PAGE
?
x * 47000, recombinant His6-myc-tagged Csg1p, SDS-PAGE
?
x * 47500, about, recombinant FLAG3-tagged enzyme, sequence calculation, x * 55000-70000, glycosylated recombinant FLAG3-tagged enzyme, SDS-PAGE
?
-
x * 47000, about, recombinant FLAG3-tagged enzyme, sequence calculation, x * 48000, glycosylated recombinant FLAG3-tagged enzyme, SDS-PAGE
-
?
-
x * 47500, about, recombinant FLAG3-tagged enzyme, sequence calculation, x * 55000-70000, glycosylated recombinant FLAG3-tagged enzyme, SDS-PAGE
-
additional information
Csg1p and Csg2p form a heterodimer that functions as a MIPC synthase
additional information
Csg1p and Csg2p form a heterodimer that functions as a MIPC synthase
additional information
-
Csg1p and Csg2p form a heterodimer that functions as a MIPC synthase
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
Csg1 is N-glycosylated with core-type structures. Deglycosylation by peptide N-glycosidase (PNGase) F. Csg2 has an effect on the glycosylation status of Csg1. Csg1 is predicted to be N-glycosylated at N224, N295, N298, N370, N379, and N380
glycoprotein
Csh1 is N-glycosylated with mannan-type structures. Deglycosylation by peptide N-glycosidase (PNGase) F. Csg2 has an effect on the glycosylation status of Csh1. Csh1 is N-glycosylated at N51 and N247
glycoprotein
Csh1p contains potential N-glycosylation sites
glycoprotein
-
Csg1 is N-glycosylated with core-type structures. Deglycosylation by peptide N-glycosidase (PNGase) F. Csg2 has an effect on the glycosylation status of Csg1. Csg1 is predicted to be N-glycosylated at N224, N295, N298, N370, N379, and N380
-
glycoprotein
-
Csh1p contains potential N-glycosylation sites
-
glycoprotein
-
Csh1 is N-glycosylated with mannan-type structures. Deglycosylation by peptide N-glycosidase (PNGase) F. Csg2 has an effect on the glycosylation status of Csh1. Csh1 is N-glycosylated at N51 and N247
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N247Q
site-directed mutagenesis, N-glycosylation of the mutant is reduced compared to the wild-type enzyme
N51Q
site-directed mutagenesis, N-glycosylation of the mutant is reduced compared to the wild-type enzyme
N51Q/N247Q
site-directed mutagenesis, N-glycosylation of the mutant is reduced compared to the wild-type enzyme
N247Q
-
site-directed mutagenesis, N-glycosylation of the mutant is reduced compared to the wild-type enzyme
-
N51Q
-
site-directed mutagenesis, N-glycosylation of the mutant is reduced compared to the wild-type enzyme
-
N51Q/N247Q
-
site-directed mutagenesis, N-glycosylation of the mutant is reduced compared to the wild-type enzyme
-
additional information
additional information
association between recombinant HA3-tagged Csg2p and His6-myc-tagged Csg1p. The N-terminally truncated Csg2p retains the Csg1p-interacting site. The small amounts of M(IP)2C-B'/B and MIPC-C observed in the DELTAcsg2 cells are completely lacking after the introduction of the DELTAcsg1 mutation. The DELTAcsg2 mutant, as well as the DELTAcsg1/DELTAcsh1 double mutant, is highly sensitive to Ca2+ and does not grow on the YPD plate medium. Overexpression of Csg1p suppresses the Ca2+-sensitive phenotype of a csg2 mutant, but in the inverse experiment, overexpression of Csg2p does not suppress the Ca2+-sensitivity of a csg1 mutant
additional information
association between recombinant HA3-tagged Csg2p and His6-myc-tagged Csg1p. The N-terminally truncated Csg2p retains the Csg1p-interacting site. The small amounts of M(IP)2C-B'/B and MIPC-C observed in the DELTAcsg2 cells are completely lacking after the introduction of the DELTAcsg1 mutation. The DELTAcsg2 mutant, as well as the DELTAcsg1/DELTAcsh1 double mutant, is highly sensitive to Ca2+ and does not grow on the YPD plate medium. Overexpression of Csg1p suppresses the Ca2+-sensitive phenotype of a csg2 mutant, but in the inverse experiment, overexpression of Csg2p does not suppress the Ca2+-sensitivity of a csg1 mutant
additional information
generation of csg1 and csg2 mutants, phenotypes, overview. The csg1DELTA strain (689DELTAcsg1) is constructed by disrupting CSG1 in DBY689 (MATa ura3-52 leu2). The isogenic csg2D (689Dcsg2) and ccc2D (689Dccc2) strains are constructed by transforming DBY689 with the CSG2- or CCC2-disrupting constructs. Cu2+ reverses the Ca2+ sensitivity of csg1 mutant cells. Kinetics of Ca2+-induced cell death, in both csg1 and csg2 mutants, Ca2+ accumulation begins after a delay of about 30 min following addition of 10 mM Ca2+. This overaccumulation phenotype is specific for Ca2+, since Sr2+ accumulation in the csg1 and csg2 mutant cells is comparable to Sr2+ accumulation by wild-type cells. Calcineurin, calmodulin and phospholipase C do not mediate the Ca2+-induced death of the csg mutants
additional information
-
generation of csg1 and csg2 mutants, phenotypes, overview. The csg1DELTA strain (689DELTAcsg1) is constructed by disrupting CSG1 in DBY689 (MATa ura3-52 leu2). The isogenic csg2D (689Dcsg2) and ccc2D (689Dccc2) strains are constructed by transforming DBY689 with the CSG2- or CCC2-disrupting constructs. Cu2+ reverses the Ca2+ sensitivity of csg1 mutant cells. Kinetics of Ca2+-induced cell death, in both csg1 and csg2 mutants, Ca2+ accumulation begins after a delay of about 30 min following addition of 10 mM Ca2+. This overaccumulation phenotype is specific for Ca2+, since Sr2+ accumulation in the csg1 and csg2 mutant cells is comparable to Sr2+ accumulation by wild-type cells. Calcineurin, calmodulin and phospholipase C do not mediate the Ca2+-induced death of the csg mutants
additional information
the DELTAcsg1/DELTAcsh1 double mutant is highly sensitive to Ca2+ and does not grow on the YPD plate medium
additional information
the DELTAcsg1/DELTAcsh1 double mutant is highly sensitive to Ca2+ and does not grow on the YPD plate medium
additional information
-
association between recombinant HA3-tagged Csg2p and His6-myc-tagged Csg1p. The N-terminally truncated Csg2p retains the Csg1p-interacting site. The small amounts of M(IP)2C-B'/B and MIPC-C observed in the DELTAcsg2 cells are completely lacking after the introduction of the DELTAcsg1 mutation. The DELTAcsg2 mutant, as well as the DELTAcsg1/DELTAcsh1 double mutant, is highly sensitive to Ca2+ and does not grow on the YPD plate medium. Overexpression of Csg1p suppresses the Ca2+-sensitive phenotype of a csg2 mutant, but in the inverse experiment, overexpression of Csg2p does not suppress the Ca2+-sensitivity of a csg1 mutant
-
additional information
-
generation of csg1 and csg2 mutants, phenotypes, overview. The csg1DELTA strain (689DELTAcsg1) is constructed by disrupting CSG1 in DBY689 (MATa ura3-52 leu2). The isogenic csg2D (689Dcsg2) and ccc2D (689Dccc2) strains are constructed by transforming DBY689 with the CSG2- or CCC2-disrupting constructs. Cu2+ reverses the Ca2+ sensitivity of csg1 mutant cells. Kinetics of Ca2+-induced cell death, in both csg1 and csg2 mutants, Ca2+ accumulation begins after a delay of about 30 min following addition of 10 mM Ca2+. This overaccumulation phenotype is specific for Ca2+, since Sr2+ accumulation in the csg1 and csg2 mutant cells is comparable to Sr2+ accumulation by wild-type cells. Calcineurin, calmodulin and phospholipase C do not mediate the Ca2+-induced death of the csg mutants
-
additional information
-
the DELTAcsg1/DELTAcsh1 double mutant is highly sensitive to Ca2+ and does not grow on the YPD plate medium
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-myc-tagged enzyme from Saccharomyces cerevisiae by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene CGS1, sequence comparisons, recombinant expression of wild-type and mutant enzymes
gene CSG1, recombinant expression of C-terminally His6-myc-tagged enzyme in Saccharomyces cerevisiae. Association between recombinant HA3-tagged Csg2p and His6-myc-tagged Csg1p
gene CSH1, recombinant expression of C-terminally His6-myc-tagged enzyme in Saccharomyces cerevisiae
recombinant expression of FLAG3-tagged enzyme in Saccharomyces cerevisiae KA31-1A (CSG1 CSH1) cells resulting in SUY69 cells, coexpression of Cgs2 Ca2+-binding protein, quantitative real-time PCR enzyme expression analysis. Csg2 has an effect on the protein level of Csg1
recombinant FLAG3-tagged wild-type and mutant enzymes in Saccharomyces cerevisiae KA31-1A (CSG1 CSH1) cells resulting in SUY73 cells, coexpression of Cgs2 Ca2+-binding protein, quantitative real-time PCR enzyme expression analysis. Csg2 has an effect on the protein level of Csh1
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Ca2+ stimulates a Csg2-dependent increase in Csg1 levels
Ca2+ stimulates a Csg2-dependent increase in Csg1 levels
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Uemura, S.; Kihara, A.; Inokuchi, J.; Igarashi, Y.
Csg1p and newly identified Csh1p function in mannosylinositol phosphorylceramide synthesis by interacting with Csg2p
J. Biol. Chem.
278
45049-45055
2003
Saccharomyces cerevisiae (P33300), Saccharomyces cerevisiae (P38287), Saccharomyces cerevisiae ATCC 204508 (P33300), Saccharomyces cerevisiae ATCC 204508 (P38287)
brenda
Uemura, S.; Kihara, A.; Iwaki, S.; Inokuchi, J.; Igarashi, Y.
Regulation of the transport and protein levels of the inositol phosphorylceramide mannosyltransferases Csg1 and Csh1 by the Ca2+-binding protein Csg2
J. Biol. Chem.
282
8613-8621
2007
Saccharomyces cerevisiae (P33300), Saccharomyces cerevisiae (P38287), Saccharomyces cerevisiae ATCC 204508 (P33300), Saccharomyces cerevisiae ATCC 204508 (P38287)
brenda
Beeler, T.; Fu, D.; Rivera, J.; Monaghan, E.; Gable, K.; Dunn, T.
SUR1 (CSG1/BCL21), a gene necessary for growth of Saccharomyces cerevisiae in the presence of high Ca2+ concentrations at 37C, is required for mannosylation of inositolphosphorylceramide
Mol. Gen. Genet.
255
570-579
1997
Saccharomyces cerevisiae (P33300), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P33300)
brenda
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