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1

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The germ tubes of Candida albicans hyphae and pseudohyphae show different patterns of septin ring localization (2001)

Sudbery, Peter E.

Oxford, UK : Blackwell Science Ltd

Molecular microbiology 41 (2001), S. 0

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ISSN: 1365-2958

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Biology , Medicine

Notes: The location of the septin ring in the germ tubes of Candida albicans hyphae and pseudohyphae was studied using an antibody to Saccharomyces cerevisiae Cdc11p. In pseudohyphae induced by growth at 35°C in YEPD or Lee's medium, a septin ring formed at or near (mean 1.8 µm) the neck between the mother cell and the germ tube. This became double later in the cycle, and the first mitosis took place across the plane of this double ring. A septin ring also formed at the germ tube neck of developing hyphae induced by serum or growth on Lee's medium at 37°C. However, at later times, this ring became disorganized and disappeared. A second double ring then appeared 10–15 µm (mean 12.5 µm) along the length of the germ tube. The nucleus subsequently migrated out of the mother cell into the germ tube, and the first mitosis took place across the plane of this second septin ring. The relocation of the septin ring in developing hyphae provides a clear-cut molecular distinction between hyphae and pseudohyphae. Commitment to one type of septin localization and mitosis was shown to occur early in the first mitotic cycle, well before evagination. Germ tubes of hyphae and pseudohyphae also have different widths. A point of commitment to germ tube width was also demonstrated, but occurred later in the cycle, approximately coincident with the time of evagination.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1046/j.1365-2958.2001.02459.x

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Genes which control cell proliferation in the yeast Saccharomyces cerevisiae (1980)

Sudbery, Peter E. ; Goodey, Andrew R. ; Carter, Bruce L. A.

[s.l.] : Nature Publishing Group

Nature 288 (1980), S. 401-404

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ISSN: 1476-4687

Source: Nature Archives 1869 - 2009

Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics

Notes: [Auszug] Small cell-size mutants of strain X2180-1A were isolated by a procedure involving cell size separation by zonal centrifugation together with the use of the mating hormone a factor. This procedure is described in detail elsewhere7. Three mutants, designated whiAl, whi C7 and whtD3, which were ...

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1038/288401a0

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3

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Expression of the α-galactosidase from Cyamopsis tetragonoloba (guar) by Hansenula polymorpha (1991)

Fellinger, Arthur J. ; Verbakel, John M. A. ; Veale, Rosemary A. ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Yeast 7 (1991), S. 463-473

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ISSN: 0749-503X

Keywords: Secretion ; methylotrophic yeast ; glycosylation ; methanol oxidase ; Life and Medical Sciences ; Genetics

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology

Notes: The methylotrophic yeast Hansenula polymorpha, a host organism for the production of heterologous proteins, has been applied to produce the α-galactosidase from the plant Cyamopsis tetragonoloba (guar). The yeast/Escherichia coli shuttle expression vector used is based on the origin of replication of the endogenous 2 μm plasmid of Saccharomyces cerevisiae and the LEU2 gene of S. cerevisiae for selection in H. polymorpha. In the expression vector, the α-galactosidase is controlled by the methanol-regulated promoter from the methanol oxidase gene, MOX, of H. polymorpha. The signal sequence of SUC2 (invertase) from the yeast S. cerevisiae, was used to ensure secretion of the α-galactosidase enzyme. After transformation and stabilization, the expression vector was stably integrated in the genome. The active α-galactosidase enzyme was efficiently secreted (〉85%) and after methanol induction, the expression level was 42 mg/l. Amino-terminal sequencing of the purified α-galactosidase enzyme synthesized by H. polymorpha showed that the S. cerevisiae invertase signal sequence was correctly processed by H. polymorpha. The secreted α-galactosidase was glycosylated and had a sugar content of 9·5%. The specific activity of the α-galactosidase produced by H. polymorpha was 38 U mg-1 compared to 100 U mg-1 for guar α-galactosidase. Deglycosylation of the H. polymorpha α-galactosidase restored the specific activity completely.

Additional Material: 5 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/yea.320070505

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4

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Expression of the glucose oxidase gene from Aspergillus niger in Hansenula polymorpha and its use as a reporter gene to isolate regulatory mutations (1993)

Hodgkins, Martin ; Sudbery, Peter ; Mead, David ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Yeast 9 (1993), S. 625-635

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ISSN: 0749-503X

Keywords: Aspergillus niger ; gene expression ; glucose oxidase ; Hansenula polymorpha ; MF-α secretion leader sequence ; methylotrophic yeast ; methanol oxidase promoter ; recombinant protein ; regulatory mutants ; reporter gene ; super-secretion mutant ; Life and Medical Sciences ; Genetics

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology

Notes: The glucose oxidase gene (god) from Aspergillus niger was expressed in Hansenula polymorpha using the methanol oxidase promoter and transcription termination region and the MF-α leader sequence from Saccharomyces cerevisiae to direct secretion. The expression cassette was cloned into the S. cerevisiae vector YEp13 and used to transform H. polymorpha strain A16. In the initial transformants plasmid replication was unstable, but was stabilized by a growth regime consisting of alternating cycles of selective and non-selective growth. The stabilized strain was grown to high cell density by fed-batch fermentation. Upon induction of the MOX promoter, glucose oxidase synthesis was initiated. At the end of the fermentation, the culture density was 76 g dry weight/1 and 108 IU/ml (0·5 g/l or 0·65% dry weight) glucose oxidase was found in the culture medium; a further 86 IU/ml (0·43 g/l or 0·56% dry weight) was recovered from the cell lysate. A plate assay was used to monitor glucose oxidase levels in individual colonies. This was then used to isolate mutants which showed abnormal regulation of god expression or which showed an altered pattern of secretion. One mutant, which showed increased production of glucose oxidase, was grown to high cell density by fed-batch fermentation (100·6 g/l) and produced 445 IU/ml (2·25 g/l or 2·2% dry weight) extracellularly and 76 IU/ml (0·38 g/l or 0·4% dry weight) intracellularly. The mutant thus not only increased total production but exported 83% of the total enzyme made compared to 55% in the parent strain.

Additional Material: 7 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/yea.320090609

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5

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Genetic analysis in the methylotrophic yeast Hansenula polymorpha (1988)

Gleeson, Martin A. ; Sudbery, Peter E.

New York, NY [u.a.] : Wiley-Blackwell

Yeast 4 (1988), S. 293-303

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ISSN: 0749-503X

Keywords: Hansenula polymorpha ; methylotrophic yeast ; genetic analysis ; methanol mutant ; Life and Medical Sciences ; Genetics

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology

Notes: Techniques are described for the induction, isolation, and characterization of mutants of Hansenula polymorpha. In addition, techniques for controlled passage through the life cycle and genetic analyses, including complementation, tetrad and random spore analysis, have been developed and used to assign mutants to 62 complementation groups. We report that organism conforms to the expected genetics of a homothallic yeast and displays a Mendelian segregation of genes through meiosis. Preliminary mapping data are presented indicating linkage of three genes on a single linkage fragment. Enymatic analysis of methanol-non-utilizing mutants identified one class which is totally deficient in the key assimilatroy enzyme, dihydroxyacetone synthase.

Additional Material: 4 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/yea.320040407

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6

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Deregulation of CLN1 and CLN2 in the Saccharomyces cerevisiae whi2 Mutant (1997)

RADCLIFFE, PIPPA ; TREVETHICK, JANET ; TYERS, MIKE ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Yeast 13 (1997), S. 707-715

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ISSN: 0749-503X

Keywords: CLN1 ; CLN2 ; CLN3 ; G1 cyclins ; stationary phase ; WHI2 ; Life and Medical Sciences ; Genetics

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology

Notes: Wild-type cells of the budding yeast Saccharomyces cerevisiae arrest in G1 upon nutrient exhaustion. Cell cycle arrest requires the WHI2 gene since whi2 mutants continue to divide and become abnormally small as nutrients are depleted. Here we show that CLN1 and CLN2 transcript levels in a whi2 strain are higher during exponential growth, and persist longer upon starvation, than in an isogenic wild-type strain. In contrast to CLN1 and CLN2, CLN3 levels declined only at very high cell density and were unaffected by the whi2 mutation. Elevated CLN expression is sufficient to explain the whi2 phenotype since ectopic expression of CLN1 in a nutrient-depleted culture caused cells to continue dividing and interfered with the acquisition of heat resistance. These observations show that, either directly or indirectly, Whi2 negatively regulates G1 cyclin expression. Interestingly extremely high levels of Cln1 induced filamentous growth upon nutrient deprivation, suggesting a direct connection between G1 cyclin activity and morphological responses to poor nutrient conditions. © 1997 John Wiley & Sons, Ltd.

Additional Material: 2 Ill.

Type of Medium: Electronic Resource

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