Phospholipid acylhydrolases trigger membrane degradation during fungal sporogenesis

Dippe, Martin; Ulbrich‐Hofmann, Renate

doi:10.1016/j.fgb.2011.05.008

Cited by 5 publications

(5 citation statements)

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“…However, no significant reaction rate (B0.3 lmol min -1 mg -1 ) was detectable with triolein or the fatty acid amide in sphingomyelin. The missing conversion of the triolein by all of the enzymes is in accordance with our findings that the crude enzyme extracts from A. ostoyae do not show any lipase activity toward triglycerides in the absence of detergents as well as in the presence of Triton X-100 or taurocholate [14]. For a detailed comparison, kinetic studies with the cleavable lipids were performed (Fig.…”

Section: Substrate Selectivity Towards Different Classes Of Lipidssupporting

confidence: 89%

“…All other phospholipids, fatty acids, fatty acid esters, enzyme inhibitors and peptide-N-glycosidase F (PNGase F) from Elizabethkingia meningoseptica were from Sigma (St. Louis, USA). Soybean fatty acids were prepared from PC as described elsewhere [14]. All other chemicals were of the highest purity commercially available.…”

Section: Methodsmentioning

confidence: 99%

“…In contrast to many enzymes produced by filamentous fungi [27], there is little information about acyl ester hydrolases from basidiomycetes. Of several basidiomycetes tested, the fruiting bodies of the species A. ostoyae were shown recently to contain high PLA 1 activity [14], therefore this species was chosen for protein purification and characterization.…”

Section: Purification Of Pla 1 Enzymes From a Ostoyae Fruiting Bodiesmentioning

confidence: 99%

“…Recently, PLA 1 activity has been found in fruiting bodies of the basidiomycete Armillaria ostoyae, which was shown to be responsible for phospholipid degradation during sporogenesis [14]. In this paper we report on the purification and characterization of this enzymatic activity yielding four new enzymes with PLA 1 activity but uncommon substrate selectivity.…”

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confidence: 92%

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Phospholipases A₁ from Armillaria ostoyae Provide Insight into the Substrate Recognition of α/β‐Hydrolase Fold Enzymes

Dippe

Müller

Sinz

et al. 2012

J Americ Oil Chem Soc

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Four enzymes with phospholipase A 1 (PLA 1 ) activity were purified from the fruiting bodies of the basidiomycete Armillaria ostoyae. The enzymes (PLA 1 -1, -2, -3 and -4) showed similar isoelectric points (4.3, 3.9, 4.0 and 4.0) and apparent molecular masses in the range of 35-47 kDa. Mass spectrometric analyses of proteolytic fragments revealed sequences homologous to a/b-hydrolase fold enzymes. The enzymes share one conserved region with fungal phospholipases B and the active site sequence with bacterial esterases and PLA 1 s. PLA 1 -1 cleaves phospholipids and lysophospholipids with an optimum activity at pH 5.3. In contrast, PLA 1 -2, -3 and -4 are characterized by broad pH optima in the slightly acidic to neutral range and are additionally capable of hydrolyzing mono-and diglycerides as well as fatty acid methyl esters. All enzymes favor glycerol-based lipids with a single medium-sized fatty acid moiety in the sn-1 position but show reduced activity towards the corresponding 1,2-diacyl derivatives with bulky long-chain or inflexible Data from mass-spectrometric peptide sequencing are available in the PRIDE database (http://www.ebi.ac.uk/pride/) under the accession numbers 17662-17665.Electronic supplementary material The online version of this article (

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Section: Substrate Selectivity Towards Different Classes Of Lipidssupporting

confidence: 89%

Section: Methodsmentioning

confidence: 99%

Section: Purification Of Pla 1 Enzymes From a Ostoyae Fruiting Bodiesmentioning

confidence: 99%

mentioning

confidence: 92%

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Phospholipases A₁ from Armillaria ostoyae Provide Insight into the Substrate Recognition of α/β‐Hydrolase Fold Enzymes

Dippe

Müller

Sinz

et al. 2012

J Americ Oil Chem Soc

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“…Of note, lysophosphatidylcholine, a typical product of PLA 2 activity, including TbSP1 (16), has been identified as a signal promoting the expression of colonization-related genes in the arbuscular mycorrhizal symbiosis (4). Also, the membrane phospholipid composition has been shown to be critical for nodule formation and symbiosis establishment by leguminous plant-symbiotic bacteria (42,43).…”

Section: Discussionmentioning

confidence: 99%

Autoproteolytic Activation of a Symbiosis-regulated Truffle Phospholipase A2

Cavazzini

Meschi

Corsini

et al. 2013

Journal of Biological Chemistry

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Background: TbSP1 is a phospholipase A 2 strongly up-regulated during the symbiotic phase of the truffle Tuber borchii. Results: An activated enzyme species composed of five ␣-helices is generated by self-proteolysis through an intermolecular reaction. Conclusion: TbSP1 autoproteolysis is a site-specific post-translational modification not involving the phospholipase active site. Significance: Autoproteolytic activation is described for the first time for a microbial PLA 2 , with possible implications for symbiosis establishment.

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Novel strategy for production of aggregation-prone proteins and lytic enzymes in Escherichia coli based on an anchored periplasmic expression system

Lee

Velmurugan

Jeong

2013

Journal of Bioscience and Bioengineering

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Phospholipid acylhydrolases trigger membrane degradation during fungal sporogenesis

Cited by 5 publications

References 49 publications

Phospholipases A₁ from Armillaria ostoyae Provide Insight into the Substrate Recognition of α/β‐Hydrolase Fold Enzymes

Phospholipases A₁ from Armillaria ostoyae Provide Insight into the Substrate Recognition of α/β‐Hydrolase Fold Enzymes

Autoproteolytic Activation of a Symbiosis-regulated Truffle Phospholipase A2

Novel strategy for production of aggregation-prone proteins and lytic enzymes in Escherichia coli based on an anchored periplasmic expression system

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Phospholipid acylhydrolases trigger membrane degradation during fungal sporogenesis

Cited by 5 publications

References 49 publications

Phospholipases A1 from Armillaria ostoyae Provide Insight into the Substrate Recognition of α/β‐Hydrolase Fold Enzymes

Phospholipases A1 from Armillaria ostoyae Provide Insight into the Substrate Recognition of α/β‐Hydrolase Fold Enzymes

Autoproteolytic Activation of a Symbiosis-regulated Truffle Phospholipase A2

Novel strategy for production of aggregation-prone proteins and lytic enzymes in Escherichia coli based on an anchored periplasmic expression system

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Phospholipases A₁ from Armillaria ostoyae Provide Insight into the Substrate Recognition of α/β‐Hydrolase Fold Enzymes

Phospholipases A₁ from Armillaria ostoyae Provide Insight into the Substrate Recognition of α/β‐Hydrolase Fold Enzymes