A Role for Saccharomyces cerevisiae Fatty Acid Activation Protein 4 in Regulating ProteinN-Myristoylation during Entry into Stationary Phase

Ashrafi, Kaveh; Farazi, Thalia A.; Gordon, Jeffrey I.

doi:10.1074/jbc.273.40.25864

Cited by 93 publications

(94 citation statements)

References 66 publications

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“…Uracil prototrophic yeast transformants were checked for the presence of pYESPDE1 by both PCR and DNA gel blot analysis (data not shown). No specific phenotype has been ascribed to the atc8⌬ mutant YB853 (Ashrafi et al, 1998), but close inspection of its growth pattern compared with that of the isogenic wild-type strain YB332 revealed that YB853 showed a longer lag phase on both glucose-and galactose-supplemented yeast peptone dextrose (YPD) medium, corresponding to 2.5 to 3 hr. To check for complementation of this growth phenotype, the following experimental protocol was followed.…”

Section: Complementation Of the S Cerevisiae Atc8⌬ Mutationmentioning

confidence: 99%

“…The atc8⌬ mutant YB853 was generated in a screen for interactions affecting the N-myristoylation pathway in yeast, but no mutant phenotype was reported in that study (Ashrafi et al, 1998) or was known to its authors (K. Ashrafi, personal communication). Therefore, we performed a detailed comparison of the growth and development of YB853 with an isogenic wild-type yeast strain YB332.…”

Section: Pde1 Encodes a P-type Atpasementioning

confidence: 99%

“…To determine whether PDE1 was functionally related to P-type ATPases of the aminophospholipid translocase group, we subcloned a 4.6-kb intronless fragment of the PDE1 gene into pYES2 for expression under the S. cerevisiae GAL1 promoter in the atc8⌬ mutant YB853 (Ashrafi et al, 1998). The atc8⌬ mutant YB853 was generated in a screen for interactions affecting the N-myristoylation pathway in yeast, but no mutant phenotype was reported in that study (Ashrafi et al, 1998) or was known to its authors (K. Ashrafi, personal communication).…”

Section: Pde1 Encodes a P-type Atpasementioning

confidence: 99%

“…Phylogenetic analysis showed that the PDE1 product is most closely related to P-type ATPases of the DRS2 family of putative aminophospholipid translocases, as shown in Figure 5B. It is clearly distinct from the other main classes of P-type ATPases, including the H ϩ -ATPases, Ca 2ϩ -ATPases, and Na ϩ -ATPases (all P 2 type), Cu 2ϩ -ATPases (P 1 type), and P 4 -type ATPases that have been identified so far (reviewed by Catty et al, 1997;Paulsen et al, 1998).To determine whether PDE1 was functionally related to P-type ATPases of the aminophospholipid translocase group, we subcloned a 4.6-kb intronless fragment of the PDE1 gene into pYES2 for expression under the S. cerevisiae GAL1 promoter in the atc8⌬ mutant YB853 (Ashrafi et al, 1998). The atc8⌬ mutant YB853 was generated in a screen for interactions affecting the N-myristoylation pathway in yeast, but no mutant phenotype was reported in that study (Ashrafi et al, 1998) or was known to its authors (K. Ashrafi, personal communication).…”

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PDE1 Encodes a P-Type ATPase Involved in Appressorium-Mediated Plant Infection by the Rice Blast Fungus Magnaporthe grisea

Balhadère

Talbot

2001

Plant Cell

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Plant infection by the rice blast fungus Magnaporthe grisea is brought about by the action of specialized infection cells called appressoria. These infection cells generate enormous turgor pressure, which is translated into an invasive force that allows a narrow penetration hypha to breach the plant cuticle. The Magnaporthe pde1 mutant was identified previously by restriction enzyme-mediated DNA integration mutagenesis and is impaired in its ability to elaborate penetration hyphae. Here we report that the pde1 mutation is the result of an insertion into the promoter of a P-type ATPase-encoding gene. Targeted gene disruption confirmed the role of PDE1 in penetration hypha development and pathogenicity but highlighted potential differences in PDE1 regulation in different Magnaporthe strains. The predicted PDE1 gene product was most similar to members of the aminophospholipid translocase group of P-type ATPases and was shown to be a functional homolog of the yeast ATPase gene ATC8 . Spatial expression studies showed that PDE1 is expressed in germinating conidia and developing appressoria. These findings implicate the action of aminophospholipid translocases in the development of penetration hyphae and the proliferation of the fungus beyond colonization of the first epidermal cell. INTRODUCTIONOne of the principal reasons why pathogenic fungi are so successful at causing plant disease is their ability to penetrate the plant cuticle directly, often using specialized infection cells called appressoria (Mendgen et al., 1996). A wide variety of fungal pathogens form appressoria, and the development of these cells involves a complex morphogenetic program that results in rapid differentiation of a highly specialized structure (Dean, 1997). The rice blast fungus Magnaporthe grisea is an important pathogen of cultivated rice and has emerged as an experimental model for the study of plant infection processes (for reviews, see Howard and Valent, 1996;Hamer and Talbot, 1998). Magnaporthe develops dome-shaped appressoria, which form at the ends of germ tubes soon after spore germination on the leaf surface. Appressoria attach strongly to the leaf and then generate enormous turgor pressure (up to 8 MPa), which is used to rupture the plant cuticle (Howard et al., 1991). The turgor inside appressoria is generated by a rapid increase in intracellular glycerol levels, which is maintained by a specialized cell wall layer containing melanin (Howard and Ferrari, 1989;de Jong et al., 1997). If melanin biosynthesis is blocked, either by chemical intervention or mutation, then Magnaporthe is unable to penetrate the plant surface and cannot cause disease (Chida and Sisler, 1987;Chumley and Valent, 1990).How such enormous cellular turgor is translated into the substantial invasive force necessary to breach the plant cell wall is not clear, but it appears to involve polarization of the cytoskeleton to the point of infection and localized cell wall modification Howard, 1990, 1992;Bechinger et al., 1999). A narrow penetration hypha forms at t...

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Section: Complementation Of the S Cerevisiae Atc8⌬ Mutationmentioning

confidence: 99%

Section: Pde1 Encodes a P-type Atpasementioning

confidence: 99%

Section: Pde1 Encodes a P-type Atpasementioning

confidence: 99%

mentioning

confidence: 99%

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PDE1 Encodes a P-Type ATPase Involved in Appressorium-Mediated Plant Infection by the Rice Blast Fungus Magnaporthe grisea

Balhadère

Talbot

2001

Plant Cell

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“…Activation of fatty acids entering S. cerevisiae can be mediated by at least four different acyl-CoA synthetase gene products, Faa1p to Faa4p (1,7,15). One of these enzymes, Faa2p, is a peroxisomal protein that carries a PTS1-like targeting sequence, while the other three enzymes do not show any obvious peroxisomal targeting sequences.…”

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confidence: 99%

Engineering the Monomer Composition of Polyhydroxyalkanoates Synthesized in Saccharomyces cerevisiae

Zhang

Carlson

Srienc

2006

Appl Environ Microbiol

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Polyhydroxyalkanoates (PHAs) have received considerable interest as renewable-resource-based, biodegradable, and biocompatible plastics with a wide range of potential applications. We have engineered the synthesis of PHA polymers composed of monomers ranging from 4 to 14 carbon atoms in either the cytosol or the peroxisome of Saccharomyces cerevisiae by harnessing intermediates of fatty acid metabolism. Cytosolic PHA production was supported by establishing in the cytosol critical ␤-oxidation chemistries which are found natively in peroxisomes. This platform was utilized to supply medium-chain (C 6 to C 14 ) PHA precursors from both fatty acid degradation and synthesis to a cytosolically expressed medium-chain-length (mcl) polymerase from Pseudomonas oleovorans. Synthesis of short-chain-length PHAs (scl-PHAs) was established in the peroxisome of a wild-type yeast strain by targeting the Ralstonia eutropha scl polymerase to the peroxisome. This strain, harboring a peroxisomally targeted scl-PHA synthase, accumulated PHA up to approximately 7% of its cell dry weight. These results indicate (i) that S. cerevisiae expressing a cytosolic mcl-PHA polymerase or a peroxisomal scl-PHA synthase can use the 3-hydroxyacyl coenzyme A intermediates from fatty acid metabolism to synthesize PHAs and (ii) that fatty acid degradation is also possible in the cytosol as ␤-oxidation might not be confined only to the peroxisomes. Polymers of even-numbered, odd-numbered, or a combination of even-and odd-numbered monomers can be controlled by feeding the appropriate substrates. This ability should permit the rational design and synthesis of polymers with desired material properties.

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Protein Recognition in Biology

McCourt

Nickels

Ishino

et al. 2007

Handbook of Biosensors and Biochips

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Protein recognition is pervasive in living systems. Interactions of proteins with each other and with other biomolecules occur in crowded and dynamic environments, ultimately leading to the multimolecular assemblies and networks that are recurrent components underpinning the molecular mechanisms of health and disease. Appreciating the nature and environment of protein interactions can help identify opportunities for molecular sensing in biological systems and guide the conditions needed for biomolecular sensing using biosensors and biochips.

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A Role for Saccharomyces cerevisiae Fatty Acid Activation Protein 4 in Regulating ProteinN-Myristoylation during Entry into Stationary Phase

Cited by 93 publications

References 66 publications

PDE1 Encodes a P-Type ATPase Involved in Appressorium-Mediated Plant Infection by the Rice Blast Fungus Magnaporthe grisea

PDE1 Encodes a P-Type ATPase Involved in Appressorium-Mediated Plant Infection by the Rice Blast Fungus Magnaporthe grisea

Engineering the Monomer Composition of Polyhydroxyalkanoates Synthesized in Saccharomyces cerevisiae

Protein Recognition in Biology

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