SYR2, A Gene Necessary for Syringomycin Growth Inhibition of Saccharomyces Cerevisiae

Cliften, Paul; Wang, Yeelan; Mochizuki, Daisuke; Miyakawa, Tokichi; Wangspa, Rungrach; Hughes, Judith M.; Takemoto, Jon Y.

doi:10.1099/13500872-142-3-477

Cited by 47 publications

(38 citation statements)

References 41 publications

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“…The C-terminal GFP fusion of the serine palmitoyltransferase-associated protein Tsc3p, the hydroxylase Sur2p, and the inositol phosphotransferase Ipt1p showed cytosolic localizations. All these proteins are described as ER-localized enzymes (7,39,40). The reason for a higher proportion of mislocalized sphingolipid enzymes was not due to the expression from an episomal plasmid but may rather reflect particular sensitivity of these enzymes to C-terminal modification and/or interference Endoplasmic reticulum (92) a ALG9, AQY1, ARE1, ARE2, AUR1, AYR1*, BOS1*, CHO1, CHO2, COX10*, CSG2*, CSR1*, CYB5, DGA1*, DPL1, DPP1*, EHT1*, ELO1, EPT1*, ERG1*, ERG2*, ERG24*, ERG25*, ERG26, ERG27*, ERG3*, ERG4, ERG5, ERG6*, ERG7*, ERG9*, EUG1*, FAA1*, FAA4*, FAT1*, FEN1, FEN2, FPS1, GAA1*, GOG5, GPI11, GPI2, GPI8, GSF2, GUP1, HMG1*, INP54*, IRE1, LCB2, LPP1*, MEC1, NCP1, NCR1, OLE1, OPI3*, PAU7*, PHO86, PIK1*, PIS1*, PLB1*, PLB2*, PTC2*, RVS161*, SAC1*, SCS7*, SEC14*, SEC22*, SLA1*, SLC1*, SPC1, STE14, SUR2, SUR4, TIP1, TSC10*, YBR204C*, YDC1*, YDL015C*, YDL193W*, YDR018C*, YIL011W, YIM1*, YJU3*, YKL174C*, YKR003W*, YLR343W, YOL132W*, YOR059C*, LCB1, YJU3*, NVJ1, YDL015C* Lipid droplets (23) AYR1*, DGA1*, EHT1*, ERG1*, ERG27*, ERG6*, ERG7*, FAA4*, FAT1*, PDR16*, SLC1*, TGL1, TGL3, YBR042C, YBR204C*, YDL193W*, YDR018C*, YIM1*, YJU3*, YKR046C, YKR089C, YOR059C*, YOR081C Peroxisomes (17) ACS1, DCI1*, FAA2*, MDH3*, PEX10, PEX11, PEX13, PEX14, PEX17*, PEX19*, PEX2*, PEX3, PEX4, PEX5*, POT1, POX1, SPS19* Plasma membrane (14) ALR1*, ERG13*, FAA1*, FAA3, GIT1*, PDR16*, PDR17*, SNQ2, TSC10*, VHT1*, YJL145W*, YLL012W, YMR210W*, YOR009W* Mitochondria (27) AAD10, ACP1, AGP2, BIO2, CEM1*, COQ1, COX10*, COX4, CPT1, CRC1, CYB2, ECM1, ERG13*, GUT1, HEM1, PGS1, PPT2*, PSD1, RAM1*, RVS167, SCS3, TES1, TGL2, YAP1, YBR159W*, YDR531W, YPR140W Vacuole, membrane (7) ALR1*, AST2*, DPP1*, PIB1, PIB2, VPH1, YBR161W* Vacuole, lumen (5) GIT1*, PKA3*, SUR1*, YIL005W, YOR009W* Nucleus, lumen (56) ACS2, ADA2*, ALD2, ARD1*, BDF1, BET2*, BET4, CDC43*, DCI1*, ERG10, ERG13*, FMS1*, GCN5, GDS1, HAP2, HAP5, HDA1, HHF1, HHT1, HHT2, HTA3*, IML3*, INO4*, MRS6*, MUQ1*, NAT1, NDD1*, PGD1*, PIP2*, PKA3*, QRI2, RAD61, RAM2*, REX3, RFA2*, RFA3*, ROX1, RPD3*, RTT105, SCM3, SEC21, SKN7, SPO12, THI3, TOR2*, TUP1*, YCR072C*, YGL144C*, YGR198W*, YHR046C*, YJR107W*, YKL091C, YLR323C, YMR192W, YNL086W*, YOL054W Nucleus, nucleolus (5) ADA2*, HTA3*, IML3*, RER2*, YCR072C* Nucleus, envelope (6) ADR1, NDD1*, NUP53, OPI1, PCT1, YPC1* Vesicles (55) APG7*, APL2*, AQY2, AST2*, BET1, BOS1*, CDC48*, CSG2*, DPP1*, ERG2*, ERG20, ERG24*, ERG25*, ERG3*, ERG9*, EUG1*, FAA1*, GAA1*, GIT1*, GTS1, HES1*, HFA1*, HMG1*, INP54*, KES1*, LPP1*, OPI3*, PAU7*, PDR5*, PIS1*, PKA3*, PLB1*, PLB2*, PLB3*, PPT2*, PTC2*, RER2*, SCS7*, SEC22*, SUR1*, TSC10*, VHT1*, VPS4*, YBR108W*, YBR161W*, YDC1*, YDL015C*, YGR198W*, YJL072C, YKL174C*, YKR003W*, YKT6, YOL132W*, YOR009W*, YPC1* Golgi (7) BET3*, EPT1*, GDA1, PIK1*, PIS1*, SAC1*, SEC14* Cytoskeleton (7) SAC6*, SLA1*, SRV2*, YGR136W, YSC84*, YDR532C*, ZTA1* Others (8) SEC2*, VPS...…”

Section: Overexpression Of Gfp Fusions Results In Stablementioning

confidence: 99%

The Spatial Organization of Lipid Synthesis in the Yeast Saccharomyces cerevisiae Derived from Large Scale Green Fluorescent Protein Tagging and High Resolution Microscopy

Natter

Leitner

Faschinger

et al. 2005

Molecular & Cellular Proteomics

160

147

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The localization pattern of proteins involved in lipid metabolism in the yeast Saccharomyces cerevisiae was determined using C-terminal green fluorescent protein tagging and high resolution confocal laser scanning microscopy. A list of 493 candidate proteins (ϳ9% of the yeast proteome) was assembled based on proteins of known function in lipid metabolism, their interacting proteins, proteins defined by genetic interactions, and regulatory factors acting on selected genes or proteins. Overall 400 (81%) transformants yielded a positive green fluorescent protein signal, and of these, 248 (62% of the 400) displayed a localization pattern that was not cytosolic. Observations for many proteins with known localization patterns were consistent with published data derived from cell fractionation or large scale localization approaches. However, in many cases, high resolution microscopy provided additional information that indicated that proteins distributed to multiple subcellular locations. The majority of tagged enzymes localized to the endoplasmic reticulum (91), but others localized to mitochondria (27), peroxisomes (17), lipid droplets (23), and vesicles (53). We assembled enzyme localization patterns for phospholipid, sterol, and sphingolipid biosynthetic pathways and propose a model, based on enzyme localization, for concerted regulation of sterol and sphingolipid metabolism that involves shuttling of key enzymes between endoplasmic reticulum, lipid droplets, vesicles, and Golgi. Molecular & Cellular Proteomics 4:662-672, 2005.Biological membranes are characterized by a highly complex mixture of lipids that are key determinants of the biophysical parameters of membranes, such as fluidity, permeability, and signaling functions. Thus, lipids affect structure and function of peripheral and integral membrane proteins, and thus play a pivotal role in organelle (membrane) function. In the yeast Saccharomyces cerevisiae, the lipid composition appears rather simple, consisting mainly of glycerophospholipids, sphingolipids, and ergosterol (1); however, recent advances in analytical techniques such as nanoelectrospray ionization tandem mass spectrometry (2) have unveiled a great degree of heterogeneity within the molecular species of phospholipids. Furthermore subcellular membranes differ not only in their lipid composition in terms of lipid classes, they are also characterized by a distinct distribution of molecular species of phospholipids (3). Because only a few membranes harbor enzymes involved in lipid synthesis, this heterogeneity may be established by localized synthesis, localized degradation, and selective trafficking of membrane lipids. Interestingly apparently "linear" pathways for the synthesis of major membrane lipids involve multiple organelles: the synthesis of phosphatidylserine by a synthase (Cho1p) occurs in the endoplasmic reticulum (ER) 1 and is followed by decarboxylation to phosphatidylethanolamine in the mitochondrial inner membrane (by Psd1p) or Golgi/vacuoles (by Psd2p). Subsequently phosphatidyletha...

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Section: Overexpression Of Gfp Fusions Results In Stablementioning

confidence: 99%

The Spatial Organization of Lipid Synthesis in the Yeast Saccharomyces cerevisiae Derived from Large Scale Green Fluorescent Protein Tagging and High Resolution Microscopy

Natter

Leitner

Faschinger

et al. 2005

Molecular & Cellular Proteomics

160

147

View full text Add to dashboard Cite

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“…Deletion of SUR2 greatly increases the resistance of cells to the Pseudomonas syringae cyclic lipodepsipeptide syringomycin (33) and to the morpholine fungicide fenpropimorph, 2 an inhibitor of several enzymes in the ergosterol synthesis pathway. As discussed above, deletion of SUR2 also suppresses the Ca 2ϩ -sensitive phenotype of csg2⌬ mutants and the pleiotropic effects of rvs161 mutations.…”

Section: S Cerevisiae Cells Do Not Require Sur2p-or Scs7p-mediated Hmentioning

confidence: 99%

Hydroxylation of Saccharomyces cerevisiae Ceramides Requires Sur2p and Scs7p

Haak

Gable

Beeler

et al. 1997

Journal of Biological Chemistry

254

301

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The Saccharomyces cerevisiae SCS7 and SUR2 genes are members of a gene family that encodes enzymes that desaturate or hydroxylate lipids. Sur2p is required for the hydroxylation of C-4 of the sphingoid moiety of ceramide, and Scs7p is required for the hydroxylation of the very long chain fatty acid. Neither SCS7 nor SUR2 are essential for growth, and lack of the Scs7p-or Sur2p-dependent hydroxylation does not prevent the synthesis of mannosyldiinositolphosphorylceramide, the mature sphingolipid found in yeast. Deletion of either gene suppresses the Ca 2؉ -sensitive phenotype of csg2⌬ mutants, which arises from overaccumulation of inositolphosphorylceramide due to a defect in sphingolipid mannosylation. Characterization of scs7 and sur2 mutants is expected to provide insight into the function of ceramide hydroxylation.

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“…In Saccharomyces cerevisiae, the C-4 hydroxyl group is introduced by the activity of a diiron-oxo-type hydroxylase encoded by the SUR2 (also known as SYR2) gene (Cliften et al, 1996;Haak et al, 1997;Grilley et al, 1998). A similar enzyme occurs in plants, and the two LCB C-4 hydroxylase genes (At1g69640 and At1g14290; Figure 1) in Arabidopsis have been shown to restore trihydroxy LCB biosynthetic ability to S. cerevisiae sur2D mutants (Sperling et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

“…S. cerevisiae mutants that lack the LCB C-4 hydroxyl group do not display growth phenotypes, indicating that this hydroxyl moiety is not an essential structural feature of S. cerevisiae sphingolipids (Haak et al, 1997). Loss of LCB C-4 hydroxylation, however, does confer resistance to the Pseudomonas syringae toxin syringomycin (Cliften et al, 1996;Grilley et al, 1998). This resistance apparently arises from alterations in the physical properties of the plasma membrane that mitigate the channel-forming activity of syringomycin (Idkowiak-Baldys et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Sphingolipid Long-Chain Base Hydroxylation Is Important for Growth and Regulation of Sphingolipid Content and Composition inArabidopsis

et al. 2008

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Sphingolipids are structural components of endomembranes and function through their metabolites as bioactive regulators of cellular processes such as programmed cell death. A characteristic feature of plant sphingolipids is their high content of trihydroxy long-chain bases (LCBs) that are produced by the LCB C-4 hydroxylase. To determine the functional significance of trihydroxy LCBs in plants, T-DNA double mutants and RNA interference suppression lines were generated for the two Arabidopsis thaliana LCB C-4 hydroxylase genes Sphingoid Base Hydroxylase1 (SBH1) and SBH2. These plants displayed reductions in growth that were dependent on the content of trihydroxy LCBs in sphingolipids. Double sbh1 sbh2 mutants, which completely lacked trihydroxy LCBs, were severely dwarfed, did not progress from vegetative to reproductive growth, and had enhanced expression of programmed cell death associated-genes. Furthermore, the total content of sphingolipids on a dry weight basis increased as the relative amounts of trihydroxy LCBs decreased. In trihydroxy LCB-null mutants, sphingolipid content was ;2.5-fold higher than that in wild-type plants. Increases in sphingolipid content resulted from the accumulation of molecular species with C16 fatty acids rather than with very-long-chain fatty acids, which are more commonly enriched in plant sphingolipids, and were accompanied by decreases in amounts of C16-containing species of chloroplast lipids. Overall, these results indicate that trihydroxy LCB synthesis plays a central role in maintaining growth and mediating the total content and fatty acid composition of sphingolipids in plants.

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SYR2, A Gene Necessary for Syringomycin Growth Inhibition of Saccharomyces Cerevisiae

Cited by 47 publications

References 41 publications

The Spatial Organization of Lipid Synthesis in the Yeast Saccharomyces cerevisiae Derived from Large Scale Green Fluorescent Protein Tagging and High Resolution Microscopy

The Spatial Organization of Lipid Synthesis in the Yeast Saccharomyces cerevisiae Derived from Large Scale Green Fluorescent Protein Tagging and High Resolution Microscopy

Hydroxylation of Saccharomyces cerevisiae Ceramides Requires Sur2p and Scs7p

Sphingolipid Long-Chain Base Hydroxylation Is Important for Growth and Regulation of Sphingolipid Content and Composition inArabidopsis

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