The Saccharomyces cerevisiae PLB1 gene encodes a protein required for lysophospholipase and phospholipase B activity.

Lee, K.S.; Patton, J L; Fido, Markus; Hines, L K; Kohlwein, Sepp D.; Paltauf, F.; Henry, Susan A.; Levin, David E.

doi:10.1016/s0021-9258(17)32081-1

Cited by 122 publications

(30 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although the motif Asn-Xaa-Ser (Thr), characteristic of potential N-glycosylation sites, was not present within the sequenced peptide fragments, Ser, Thr and Asn residues were relatively abundant. All fungal phospholipases studied thus far have been glycosylated [13,14,16,21]. Deglycosylation of the protein by PNGase F resulted in almost total loss of enzyme activity, indicating that the N-linked carbohydrate moiety is important in the catalytic capability of the protein.…”

Section: Discussionmentioning

confidence: 99%

“…Cryptococcal PLB, LPL and LPTA exhibited, in general, 10-200-fold higher specific activities than the corresponding enzymes from non-pathogenic fungi [11][12][13]15,16]. LPL and LPTA activities were 100-500 fold greater than those of mammalian lysophospholipases [43,44].…”

Section: Discussionmentioning

confidence: 99%

“…Secretory phospholipases, well-known for their destructive effects on biological tissue, have been implicated in the pathogenesis of bacterial infections [9,10]. Studies of fungal phos-pholipases, however, have mainly focused on the characterization of phospholipase B (PLB ; EC 3.1.1.5) from non-pathogenic fungi, including Saccharomyces cere isiae, Torulaspora delbrueckii, Schizosaccharomyces pombe and Penicillium notatum [11][12][13][14][15][16]. In some instances, lysophospholipase (LPL ; EC 3.1.1.5) and lysophospholipase\transacylase (LPTA ; EC 3.1.1.5) activities have also been described [11,13,16], but the biological functions of these phospholipases remain undetermined.…”

Section: Introductionmentioning

confidence: 99%

“…Studies of fungal phos-pholipases, however, have mainly focused on the characterization of phospholipase B (PLB ; EC 3.1.1.5) from non-pathogenic fungi, including Saccharomyces cere isiae, Torulaspora delbrueckii, Schizosaccharomyces pombe and Penicillium notatum [11][12][13][14][15][16]. In some instances, lysophospholipase (LPL ; EC 3.1.1.5) and lysophospholipase\transacylase (LPTA ; EC 3.1.1.5) activities have also been described [11,13,16], but the biological functions of these phospholipases remain undetermined. Furthermore, the relative activities of PLB, LPL and LPTA vary between different fungal genera.…”

Section: Introductionmentioning

confidence: 99%

“…Furthermore, the relative activities of PLB, LPL and LPTA vary between different fungal genera. The terms PLB, LPL and\or LPTA have been used interchangeably [13,16], making attempts at comparison of enzyme properties difficult. Saito et al proposed that LPL is an artifact produced by proteolysis of PLB, since PLB activity was lost almost completely, with the preservation of LPL activity, during purification of phospholipases from P. notatum [11].…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Purification and characterization of secretory phospholipase B, lysophospholipase and lysophospholipase/transacylase from a virulent strain of the pathogenic fungus Cryptococcus neoformans

Chen

Wright

Golding³

et al. 2000

Biochem. J.

View full text Add to dashboard Cite

Infection caused by the fungus Cryptococcus neoformans is potentially fatal. A highly active extracellular phospholipase, demonstrating phospholipase B (PLB), lysophospholipase (LPL) and lysophospholipase/transacylase (LPTA) activities, was purified to homogeneity from C. neoformans using (NH(4))(2)SO(4) fractionation, and hydrophobic-interaction, anion-exchange and gel-filtration chromatography. All three enzyme activities co-purified as a single protein with an apparent molecular mass of 70-90 kDa by SDS/PAGE and 160-180 kDa by gel filtration. The ratio of the three activities remained constant after each purification step. The amino acid composition, as well as the sequences of the N-terminus and of five internal peptide fragments were novel. The protein was an acidic glycoprotein containing N-linked carbohydrate moieties, with pI values of 5.5 and 3.5. The apparent V(max) values for PLB and LPL activities were 12.3 and 870 micromol/min per mg of protein respectively; the corresponding K(m) values were approx. 185.3 and 92.2 microM. The enzyme was active only at acidic pH (pH optimum of 4.0 for PLB and 4.0-5.0 for LPL and LPTA). Enzyme activity did not require added cations, but was inhibited by Fe(3+). LPL and LPTA activities were decreased by 0.1% (v/v) Triton X-100 to 50% of the control value. Palmitoylcarnitine (0.5 mM) inhibited PLB (97% inhibition) and LPL and LPTA activities (35% inhibition) competitively. All phospholipids except phosphatidic acid were degraded by PLB, but dipalmitoyl phosphatidylcholine and dioleoyl phosphatidylcholine were the preferred substrates. This is the first complete description of the purification and properties of a phospholipase, which may be involved in virulence, from a pathogenic fungus.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Purification and characterization of secretory phospholipase B, lysophospholipase and lysophospholipase/transacylase from a virulent strain of the pathogenic fungus Cryptococcus neoformans

Chen

Wright

Golding³

et al. 2000

Biochem. J.

View full text Add to dashboard Cite

show abstract

In silicio identification of glycosyl-phosphatidylinositol-anchored plasma-membrane and cell wall proteins ofSaccharomyces cerevisiae

Caro

Tettelin

Vossen

et al. 1997

Yeast

316

325

View full text Add to dashboard Cite

Use of the Von Heijne algorithm allowed the identification of 686 open reading frames (ORFs) in the genome of Saccharomyces cerevisiae that encode proteins with a potential N-terminal signal sequence for entering the secretory pathway. On further analysis, 51 of these proteins contain a potential glycosyl-phosphatidylinositol (GPI)attachment signal. Seven additional ORFs were found to belong to this group. Upon examination of the possible GPI-attachment sites, it was found that in yeast the most probable amino acids for GPI-attachment are asparagine and glycine.In yeast, GPI-proteins are found at the cell surface, either attached to the plasma-membrane or as an intrinsic part of the cell wall. It was noted that plasma-membrane GPI-proteins possess a dibasic residue motif just before their predicted GPI-attachment site. Based on this, and on homologies between proteins, families of plasma-membrane and cell wall proteins were assigned, revealing 20 potential plasma-membrane and 38 potential cell wall proteins. For members of three plasma-membrane protein families, a function has been described. On the other hand, most of the cell wall proteins seem to be structural components of the wall, responsive to different growth conditions.The GPI-attachment site of yeast slightly differs from mammalian cells. This might be of use in the development of anti-fungal drugs. 1997 John Wiley & Sons, Ltd.

show abstract

Biochemistry, cell biology and molecular biology of lipids ofSaccharomyces cerevisiae

Daum

Lees

Bard

et al. 1998

Yeast

580

380

View full text Add to dashboard Cite

The yeast Saccharomyces cerevisiae is a powerful experimental system to study biochemical, cell biological and molecular biological aspects of lipid synthesis. Most but not all genes encoding enzymes involved in fatty acid, phospholipid, sterol or sphingolipid biosynthesis of this unicellular eukaryote have been cloned, and many gene products have been functionally characterized. Less information is available about genes and gene products governing the transport of lipids between organelles and within membranes, turnover and degradation of complex lipids, regulation of lipid biosynthesis, and linkage of lipid metabolism to other cellular processes. Here we summarize current knowledge about lipid biosynthetic pathways in S. cerevisiae and describe the characteristic features of the gene products involved. We focus on recent discoveries in these fields and address questions on the regulation of lipid synthesis, subcellular localization of lipid biosynthetic steps, cross‐talk between organelles during lipid synthesis and subcellular distribution of lipids. Finally, we discuss distinct functions of certain key lipids and their possible roles in cellular processes. © 1998 John Wiley & Sons, Ltd.

show abstract

The Saccharomyces cerevisiae PLB1 gene encodes a protein required for lysophospholipase and phospholipase B activity.

Cited by 122 publications

References 33 publications

Purification and characterization of secretory phospholipase B, lysophospholipase and lysophospholipase/transacylase from a virulent strain of the pathogenic fungus Cryptococcus neoformans

Purification and characterization of secretory phospholipase B, lysophospholipase and lysophospholipase/transacylase from a virulent strain of the pathogenic fungus Cryptococcus neoformans

In silicio identification of glycosyl-phosphatidylinositol-anchored plasma-membrane and cell wall proteins ofSaccharomyces cerevisiae

Biochemistry, cell biology and molecular biology of lipids ofSaccharomyces cerevisiae

Contact Info

Product

Resources

About