ライフサイエンスコーパス: Podospora

1 in yeast are infectious when introduced into Podospora.

2 nt independent discovery of ST production in Podospora [1], suggest that this HGT event probably resu

3 te Ustilago maydis (UmAbf62A) and ascomycete Podospora anserina (PaAbf62A).

4 four prions of Saccharomyces cerevisiae and Podospora anserina affect diverse biological processes:

5 ls of recombinant prion proteins from yeast, Podospora anserina and mammals can induce prion phenotyp

6 ays in the genomes of the coprophilous fungi Podospora anserina and Sordaria macrospora.

7 MAGA, and CPG-2 from the saprophytic fungus Podospora anserina and the pathogenic fungi Magnaporthe

8 sidues 218-289 of the HET-s prion protein of Podospora anserina by factors of three or more, indicati

9 4-mannanases from the coprophilic ascomycete Podospora anserina contribute to the enzymatic degradati

10 r (native Histoplasma gene or a heterologous Podospora anserina gene).

11 e loop in the position where PansMan26A from Podospora anserina has an alpha-helix (alpha9) which int

12 glutamine/asparagine (Q/N)-rich regions, the Podospora anserina HET-s and PrP prion proteins lack suc

13 GLTP, we recently showed that HET-C2 GLTP of Podospora anserina is organized conformationally as a GL

14 s are plainly diseases, the [Het-s] prion of Podospora anserina may be a functional amyloid, with imp

15 In its prion form, the HET-s protein of Podospora anserina participates in a fungal self/non-sel

16 The HET-s prion protein from the fungus Podospora anserina represents a model system to study th

17 e mitochondria from the aging model organism Podospora anserina revealed profound age-dependent chang

18 It is unclear how het gene products of Podospora anserina trigger heterokaryon incompatibility.

19 iscovered that a complete ST gene cluster in Podospora anserina was horizontally transferred from Asp

20 identified in this fashion, PODANSg2158 from Podospora anserina was selected for expression and chara

21 orecognition genes in the filamentous fungus Podospora anserina We show that the cytotoxic activity o

22 HET-s is a prion protein of the fungus Podospora anserina which, in the prion state, is active

23 han that of their homologs in another fungus Podospora anserina with a well-characterized senescence.

24 are pathogenic (unlike the [Het-s] prion of Podospora anserina), and most are amyloid-based with the

25 In the filamentous fungus Podospora anserina, a well established aging model, the

26 to Het-E1 (vegetative incompatibility) from Podospora anserina, acylaminoacyl-peptidase from Bacillu

27 e.g., mammalian PrP and the [Het-s] prion of Podospora anserina, although still able to form infectio

28 l amyloid aggregate in the filamentous fungi Podospora anserina, and is involved in mediating heterok

29 o fungi models, Saccharomyces cerevisiae and Podospora anserina, previously transformed to express Ab

30 originating from different species, namely, Podospora anserina, Puccinia graminis f. sp. tritici, an

31 In natural populations of Podospora anserina, seven spore killer types (Psks) have

32 ora species; and two spore-killer systems in Podospora anserina, Spok and [Het-s].

33 ctivator, incompatibility locus protein from Podospora anserina, telomerase-associated protein) domai

34 In Podospora anserina, the simultaneous presence of [Het-s]

35 l death was also observed in the native host Podospora anserina.

36 [Het-s] is a prion of the fungus Podospora anserina.

37 esis and caryogamy in the filamentous fungus Podospora anserina.

38 Phylogenetic analysis shows that most Podospora cluster genes are adjacent to or nested within

39 Furthermore, the Podospora cluster is highly conserved in content, sequen

40 Examination of approximately 52,000 Podospora expressed sequence tags identified transcripts