Inactivation of the Podospora anserina vegetative incompatibility locus het-c, whose product resembles a glycolipid transfer protein, drastically impairs ascospore production.

Saupe, Sven J.; Descamps, Cecile; Turcq, Béatrice; Bégueret, Joël

doi:10.1073/pnas.91.13.5927

Cited by 95 publications

(89 citation statements)

References 31 publications

(26 reference statements)

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“…sequence homology between HET-C2 and porcine GLTP was first noted by Saupe et al (5). Subsequently, glycolipid intermembrane transfer by HET-C2 was shown with radiolabeled and fluorescently labeled galactosylceramide (7).…”

Section: Structure and Glycolipid Specificity Of Het-c2-limitedmentioning

confidence: 99%

“…het genes exhibit extensive polymorphism and generally encode proteins carrying a HET domain (1)(2)(3)(4). Originally, this domain was linked to the het-c2 gene of P. anserina, where it was shown to encode a protein similar in size and with limited sequence homology to mammalian glycolipid transfer proteins (GLTPs) 5 (5,6). HET-C2 was shown to stimulate in vitro inter-membrane transfer of galactosylceramide, but not sphingomyelin, ceramide, phosphatidylcholine, or cholesterol (7).…”

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confidence: 99%

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Structural Determination and Tryptophan Fluorescence of Heterokaryon Incompatibility C2 Protein (HET-C2), a Fungal Glycolipid Transfer Protein (GLTP), Provide Novel Insights into Glycolipid Specificity and Membrane Interaction by the GLTP Fold

Kenoth

Simanshu

Kamlekar

et al. 2010

Journal of Biological Chemistry

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HET-C2 is a fungal protein that transfers glycosphingolipids between membranes and has limited sequence homology with human glycolipid transfer protein (GLTP). The human GLTP fold is unique among lipid binding/transfer proteins, defining the GLTP superfamily. Herein, GLTP fold formation by HET-C2, its glycolipid transfer specificity, and the functional role(s) of its two Trp residues have been investigated. X-ray diffraction (1.9 Å ) revealed a GLTP fold with all key sugar headgroup recognition residues (Asp 66 , Asn 70 , Lys 73 , Trp 109 , and His 147 ) conserved and properly oriented for glycolipid binding. Far-UV CD showed secondary structure dominated by ␣-helices and a cooperative thermal unfolding transition of 49°C, features consistent with a GLTP fold. Environmentally induced optical activity of Trp/Tyr/Phe (2:4:12) detected by near-UV CD was unaffected by membranes containing glycolipid but was slightly altered by membranes lacking glycolipid. Trp fluorescence was maximal at ϳ355 nm and accessible to aqueous quenchers, indicating free exposure to the aqueous milieu and consistent with surface localization of the two Trps. Interaction with membranes lacking glycolipid triggered significant decreases in Trp emission intensity but lesser than decreases induced by membranes containing glycolipid. Binding of glycolipid (confirmed by electrospray injection mass spectrometry) resulted in a blue-shifted emission wavelength maximum (ϳ6 nm) permitting determination of binding affinities. The unique positioning of Trp 208 at the HET-C2 C terminus revealed membrane-induced conformational changes that precede glycolipid uptake, whereas key differences in residues of the sugar headgroup recognition center accounted for altered glycolipid specificity and suggested evolutionary adaptation for the simpler glycosphingolipid compositions of filamentous fungi.Self/nonself recognition is a universally important process, encompassing intercellular interactions ranging from vertebrate immune responses to somatic chimera formation in protists, filamentous fungi, sponges, ascidians, and tunicates. Self/ nonself discrimination becomes critical for filamentous fungi during hyphal fusion, which enables the exchange of cytoplasm and nuclei during the assimilative growth phase (1-4). Nonself recognition triggers a postfusion, programmed cell death process known as vegetative incompatibility, which leads to heterokaryon death. The benefits of vegetative incompatibility include prevention of transmission of deleterious cytoplasmic elements (i.e. viruses) as well as restriction of plundering by parasitic genotypes.het genes are known to play a major role in vegetative incompatibility processes that occur in Neurospora crassa and Podospora anserina. het genes exhibit extensive polymorphism and generally encode proteins carrying a HET domain (1-4). Originally, this domain was linked to the het-c2 gene of P. anserina, where it was shown to encode a protein similar in size and with limited sequence homology to mammalian glycolipid transfer...

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Section: Structure and Glycolipid Specificity Of Het-c2-limitedmentioning

confidence: 99%

mentioning

confidence: 99%

Structural Determination and Tryptophan Fluorescence of Heterokaryon Incompatibility C2 Protein (HET-C2), a Fungal Glycolipid Transfer Protein (GLTP), Provide Novel Insights into Glycolipid Specificity and Membrane Interaction by the GLTP Fold

Kenoth

Simanshu

Kamlekar

et al. 2010

Journal of Biological Chemistry

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“…These proteins have been isolated from different sources ranging from spinach chloroplasts to mammalian brain, liver and kidney (Brown et al, 1990;Sasaki, 1985Sasaki, , 1990. GLTP orthologs in fungi and plants were found to be involved in programmed cell death (Brodersen et al, 2002;Mattjus et al, 2003;Saupe et al, 1994) but their function in mammals is largely unknown. The activity of GLTP is preserved after expression in E. coli (Godi et al, 2004;Lin et al, 2000;Malinina et al, 2004;Rao et al, 2004) allowing for detailed structureefunction studies in vitro.…”

Section: Introductionmentioning

confidence: 99%

Glycolipid transfer protein: Clear structure and activity, but enigmatic function

Neumann

Opacic

Wechselberger

et al. 2008

Advances in Enzyme Regulation

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“…Genome analysis revealed a second GLTP gene in humans, but it is not transcriptionally active (Zou et al, 2008). In fungi and plants, GLTP homologs have been implicated in apoptosis (Saupe et al, 1994;Brodersen et al, 2002). However, the function of GLTP in mammalian cells still remains to be explored.…”

Section: Synthesis Of Higher Glycosphingolipids Is Also Regulated By mentioning

confidence: 99%

Sphingolipid management by an orchestra of lipid transfer proteins

Neumann

Meer

2008

BCHM

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The various membranes in eukaryotic cells have unique lipid compositions. Despite important discoveries in lipid research over recent decades, the basic principles by which cells define their membrane compositions are essentially unknown. Cells must sense the concentration of each lipid, integrate such signals and regulate the activity of their metabolic enzymes and transport routes to dynamically meet their needs in terms of membrane composition. Sphingolipids constitute a lipid category that is essential for eukaryotic life and appears to be key to differences in lipid composition. Here we discuss recent findings that assign an important role to lipid transfer proteins in the regulation of sphingolipid metabolism, organization and function.

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Inactivation of the Podospora anserina vegetative incompatibility locus het-c, whose product resembles a glycolipid transfer protein, drastically impairs ascospore production.

Abstract: The het-c l contc a different alleles that elicit nelic vegetative incompatibility through specific interactions with alleles of the unlinked loci het-e and het-d.

Cited by 95 publications

References 31 publications

Structural Determination and Tryptophan Fluorescence of Heterokaryon Incompatibility C2 Protein (HET-C2), a Fungal Glycolipid Transfer Protein (GLTP), Provide Novel Insights into Glycolipid Specificity and Membrane Interaction by the GLTP Fold

Structural Determination and Tryptophan Fluorescence of Heterokaryon Incompatibility C2 Protein (HET-C2), a Fungal Glycolipid Transfer Protein (GLTP), Provide Novel Insights into Glycolipid Specificity and Membrane Interaction by the GLTP Fold

Glycolipid transfer protein: Clear structure and activity, but enigmatic function

Sphingolipid management by an orchestra of lipid transfer proteins

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