Podospora Anserina Bibliography N° 10 - Additions
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Prpsc Prions State of the Art
Sc PrP Prions State of the Art Edited by Joaquín Castilla and Jesús R. Requena Printed Edition of the Special Issue Published in Pathogens www.mdpi.com/journal/pathogens PrPSc Prions: State of the Art Sc PrP Prions: State of the Art Special Issue Editors Joaqu´ınCastilla Jes ´usR. Requena MDPI • Basel • Beijing • Wuhan • Barcelona • Belgrade Special Issue Editors Joaqu´ın Castilla Jes us´ R. Requena CIC bioGUNE University of Santiago de Compostela Spain Spain Editorial Office MDPI St. Alban-Anlage 66 Basel, Switzerland This is a reprint of articles from the Special Issue published online in the open access journal Pathogens (ISSN 2076-0817) from 2017 to 2018 (available at: https://www.mdpi.com/journal/pathogens/ special issues/prions study) For citation purposes, cite each article independently as indicated on the article page online and as indicated below: LastName, A.A.; LastName, B.B.; LastName, C.C. Article Title. Journal Name Year, Article Number, Page Range. ISBN 978-3-03897-308-9 (Pbk) ISBN 978-3-03897-309-6 (PDF) Cover image courtesy of Jesus´ R. Requena and Joaqu´ın Castilla. Articles in this volume are Open Access and distributed under the Creative Commons Attribution (CC BY) license, which allows users to download, copy and build upon published articles even for commercial purposes, as long as the author and publisher are properly credited, which ensures maximum dissemination and a wider impact of our publications. The book taken as a whole is c 2018 MDPI, Basel, Switzerland, distributed under the terms and conditions of the Creative Commons license CC BY-NC-ND (http://creativecommons.org/licenses/by-nc-nd/4.0/). -
Ascomyceteorg 08-03 Ascomyceteorg
Podospora bullata, a new homothallic ascomycete from kangaroo dung in Australia Ann BELL Abstract: Podospora bullata sp. nov. is described and illustrated based on five kangaroo dung collections Dan MAHONEY from Australia. The species is placed in the genus Podospora based on its teleomorph morphology and its Robert DEBUCHY ITS sequence from a fertile homothallic axenic culture. Perithecial necks are adorned with prominent simple unswollen filiform flexuous and non-agglutinated greyish hairs. Ascospores are characterized by minute pe- dicels, lack of caudae and an enveloping frothy gelatinous material with bubble-like structures both in the Ascomycete.org, 8 (3) : 111-118. amorphous gel and attached to the ascospore dark cell. No anamorph was observed. Mai 2016 Keywords: coprophilous fungi, Lasiosphaeriaceae, Podospora, ribosomal DNA, taxonomy. Mise en ligne le 05/05/2016 Résumé : Podospora bullata sp. nov. est une nouvelle espèce qui a été trouvée sur cinq isolats provenant d’Australie et obtenus à partir de déjections de kangourou. Cette nouvelle espèce est décrite ici avec des il- lustrations. Cet ascomycète est placé dans le genre Podospora en se basant sur la séquence des ITS et sur l’aspect de son téléomorphe, en l’occurrence un individu homothallique fertile en culture axénique. Les cols des périthèces sont ornés par une touffe de longs poils grisâtres fins, flexueux, en majorité sans ramification et non agglutinés. Les ascospores sont caractérisées par de courts pédicelles et une absence d’appendices. Les ascospores matures sont noires et entourées par un mucilage contenant des inclusions ayant l’aspect de bulles, adjacentes à la paroi de l’ascospore. -
Ami1, an Orthologue of the Aspergillus Nidulans Apsa Gene, Is Involved in Nuclear Migration Events Throughout the Life Cycle of Podospora Anserina
Copyright 2000 by the Genetics Society of America ami1, an Orthologue of the Aspergillus nidulans apsA Gene, Is Involved in Nuclear Migration Events Throughout the Life Cycle of Podospora anserina Fatima GraõÈa, VeÂronique Berteaux-Lecellier, Denise Zickler and Marguerite Picard Institut de GeÂneÂtique et Microbiologie de l'Universite Paris-Sud (Orsay), 91405 France Manuscript received September 22, 1999 Accepted for publication February 3, 2000 ABSTRACT The Podospora anserina ami1-1 mutant was identi®ed as a male-sterile strain. Microconidia (which act as male gametes) form, but are anucleate. Paraphysae from the perithecium beaks are also anucleate when ami1-1 is used as the female partner in a cross. Furthermore, in crosses heterozygous for ami1-1, some crozier cells are uninucleate rather than binucleate. In addition to these nuclear migration defects, which occur at the transition between syncytial and cellular states, ami1-1 causes abnormal distribution of the nuclei in both mycelial ®laments and asci. Finally, an ami1-1 strain bearing information for both mating types is unable to self-fertilize. The ami1 gene is an orthologue of the Aspergillus nidulans apsA gene, which controls nuclear positioning in ®laments and during conidiogenesis (at the syncytial/cellular transition). The ApsA and AMI1 proteins display 42% identity and share structural features. The apsA gene comple- ments some ami1-1 defects: it increases the percentage of nucleate microconidia and restores self-fertility in an ami1-1 matϩ (matϪ) strain. The latter effect is puzzling, since in apsA null mutants sexual reproduction is quite normal. The functional differences between the two genes are discussed with respect to their possible history in these two fungi, which are very distant in terms of evolution. -
Prions As Protein-Based Genetic Elements
14 Aug 2002 14:0 AR AR168-MI56-28.tex AR168-MI56-28.sgm LaTeX2e(2002/01/18) P1: IBD 10.1146/annurev.micro.56.013002.100603 Annu. Rev. Microbiol. 2002. 56:703–41 doi: 10.1146/annurev.micro.56.013002.100603 Copyright c 2002 by Annual Reviews. All rights reserved First published online as a Review in Advance on July 15, 2002 PRIONS AS PROTEIN-BASED GENETIC ELEMENTS Susan M. Uptain1 and Susan Lindquist2 1Howard Hughes Medical Institute, Department of Molecular Genetics and Cell Biology, University of Chicago, Chicago, Illinois 60637; e-mail: [email protected] 2Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Biology, Nine Cambridge Center, Cambridge, Massachusetts 02142; e-mail: lindquist [email protected] Key Words Sup35, Ure2, HET-s, Rnq1, amyloid ■ Abstract Fungal prions are fascinating protein-based genetic elements. They alter cellular phenotypes through self-perpetuating changes in protein conformation and are cytoplasmically partitioned from mother cell to daughter. The four prions of Saccharomyces cerevisiae and Podospora anserina affect diverse biological pro- cesses: translational termination, nitrogen regulation, inducibility of other prions, and heterokaryon incompatibility. They share many attributes, including unusual genetic behaviors, that establish criteria to identify new prions. Indeed, other fungal traits that baffled microbiologists meet some of these criteria and might be caused by prions. Recent research has provided notable insight about how prions are induced and prop- agated and their many biological roles. The ability to become a prion appears to be evolutionarily conserved in two cases. [PSI+] provides a mechanism for genetic vari- ation and phenotypic diversity in response to changing environments. -
Ribosomal RNA Modulates Aggregation of the Podospora Prion Protein HET-S
International Journal of Molecular Sciences Article Ribosomal RNA Modulates Aggregation of the Podospora Prion Protein HET-s Yanhong Pang y, Petar Kovachev and Suparna Sanyal * Department of Cell and Molecular Biology, Uppsala University, Box-596, Biomedical Center, 751 24 Uppsala, Sweden; [email protected] (Y.P.); [email protected] (P.K.) * Correspondence: [email protected] Present address: Department of Molecular Sciences, Uppsala Biocenter, Swedish University of Agricultural y Sciences, 750 07 Uppsala, Sweden. Received: 25 August 2020; Accepted: 28 August 2020; Published: 1 September 2020 Abstract: The role of the nucleic acids in prion aggregation/disaggregation is becoming more and more evident. Here, using HET-s prion from fungi Podospora anserina (P. anserina) as a model system, we studied the role of RNA, particularly of different domains of the ribosomal RNA (rRNA), in its aggregation process. Our results using Rayleigh light scattering, Thioflavin T (ThT) binding, transmission electron microscopy (TEM) and cross-seeding assay show that rRNA, in particular the domain V of the major rRNA from the large subunit of the ribosome, substantially prevents insoluble amyloid and amorphous aggregation of the HET-s prion in a concentration-dependent manner. Instead, it facilitates the formation of the soluble oligomeric “seeds”, which are capable of promoting de novo HET-s aggregation. The sites of interactions of the HET-s prion protein on domain V rRNA were identified by primer extension analysis followed by UV-crosslinking, which overlap with the sites previously identified for the protein-folding activity of the ribosome (PFAR). This study clarifies a missing link between the rRNA-based PFAR and the mode of propagation of the fungal prions. -
Drivers of Evolutionary Change in Podospora Anserina
Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology 1923 Drivers of evolutionary change in Podospora anserina SANDRA LORENA AMENT-VELÁSQUEZ ACTA UNIVERSITATIS UPSALIENSIS ISSN 1651-6214 ISBN 978-91-513-0921-7 UPPSALA urn:nbn:se:uu:diva-407766 2020 Dissertation presented at Uppsala University to be publicly examined in Ekmansalen, Evolutionary Biology Centre (EBC), Norbyvägen 18D, Uppsala, Tuesday, 19 May 2020 at 10:00 for the degree of Doctor of Philosophy (Faculty of Theology). The examination will be conducted in English. Faculty examiner: Professor Bengt Olle Bengtsson (Lund University). Abstract Ament-Velásquez, S. L. 2020. Drivers of evolutionary change in Podospora anserina. Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology 1923. 63 pp. Uppsala: Acta Universitatis Upsaliensis. ISBN 978-91-513-0921-7. Genomic diversity is shaped by a myriad of forces acting in different directions. Some genes work in concert with the interests of the organism, often shaped by natural selection, while others follow their own interests. The latter genes are considered “selfish”, behaving either neutrally to the host, or causing it harm. In this thesis, I focused on genes that have substantial fitness effects on the fungus Podospora anserina and relatives, but whose effects are very contrasting. In Papers I and II, I explored the evolution of a particular type of selfish genetic elements that cause meiotic drive. Meiotic drivers manipulate the outcome of meiosis to achieve overrepresentation in the progeny, thus increasing their likelihood of invading and propagating in a population. In P. anserina there are multiple meiotic drivers but their genetic basis was previously unknown. -
How Do Yeast Cells Contend with Prions?
International Journal of Molecular Sciences Review How Do Yeast Cells Contend with Prions? Reed B. Wickner *, Herman K. Edskes, Moonil Son, Songsong Wu and Madaleine Niznikiewicz Laboratory of Biochemistry and Genetics, National Institute of Diabetes Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, USA; [email protected] (H.K.E.); [email protected] (M.S.); [email protected] (S.W.); [email protected] (M.N.) * Correspondence: [email protected]; Tel.: +1-301-496-3452 Received: 15 June 2020; Accepted: 30 June 2020; Published: 3 July 2020 Abstract: Infectious proteins (prions) include an array of human (mammalian) and yeast amyloid diseases in which a protein or peptide forms a linear β-sheet-rich filament, at least one functional amyloid prion, and two functional infectious proteins unrelated to amyloid. In Saccharomyces cerevisiae, at least eight anti-prion systems deal with pathogenic amyloid yeast prions by (1) blocking their generation (Ssb1,2, Ssz1, Zuo1), (2) curing most variants as they arise (Btn2, Cur1, Hsp104, Upf1,2,3, Siw14), and (3) limiting the pathogenicity of variants that do arise and propagate (Sis1, Lug1). Known mechanisms include facilitating proper folding of the prion protein (Ssb1,2, Ssz1, Zuo1), producing highly asymmetric segregation of prion filaments in mitosis (Btn2, Hsp104), competing with the amyloid filaments for prion protein monomers (Upf1,2,3), and regulation of levels of inositol polyphosphates (Siw14). It is hoped that the discovery of yeast anti-prion systems and elucidation of their mechanisms will facilitate finding analogous or homologous systems in humans, whose manipulation may be useful in treatment. -
Signature Redacted. Amy E
A genetic platform for the study of protein perturbation and prion-based inheritance by Gregory A. Newby B.S., Biological Sciences Carnegie Mellon University (2009) SUBMITTED TO THE DEPARTMENT OF BIOLOGY IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF DOCTOR OF PHILOSOPHY AT THE MASSACHUSETTS INSTITUTE OF TECHNOLOGY June 2017 Massachusetts Institute of Technology 2017. All rights reserved. Signature redacted Signature of Author................................. Department of Biology redacted C e rtifie d B y .. Signature ............... I.R..... F..... / Gerald R. Fink Professor of Biology Acting Thesis Supervisor in Place of Susan Lipdquist (deceased) Accepted By............ Signature redacted. Amy E. Keating MASSACHUSETTS INSTITUTE Professor of Biology OF TECHNOLOGY Chair, Graduate Student Committee MAY 2 3 2017 LIBRARIES I 1 2 A genetic platform for the study of protein perturbation and prion-based inheritance By Gregory Arthur Newby Submitted to the Department of Biology in Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy in Biology SUMMARY Proteins mediate every cellular process. In order for life to exist, each protein must be finely tuned to carry out its function at the proper time and place. Because the environment is dynamic and often unpredictable, the regulation of proteins must be responsive to environmental stimuli. Mutations, age, and severe or repeated insults can decrease the quality of protein regulation, leading to disease. The study of protein regulation and its dysfunction in disease are of vital importance. Regulatory and disease phenomena involving protein assembly or aggregation are common but currently understudied on account of their intractability with existing techniques. In order to equip scientists with better tools to tackle these difficult phenomena, my collaborators Ahmad Khalil and Szilvia Kiriakov (Boston University) and I developed the yTRAP platform (standing for: yeast transcriptional reporters of aggregating proteins). -
The Role of RNA in Prion Aggregation and Disease
Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology 1620 The role of RNA in prion aggregation and disease PETAR STEFANOV KOVACHEV ACTA UNIVERSITATIS UPSALIENSIS ISSN 1651-6214 ISBN 978-91-513-0208-9 UPPSALA urn:nbn:se:uu:diva-338857 2018 Dissertation presented at Uppsala University to be publicly examined in A1:107a, BMC, Husargatan 3, Uppsala, Friday, 2 March 2018 at 09:00 for the degree of Doctor of Philosophy. The examination will be conducted in English. Faculty examiner: Associate professor Magnus Wolf-Watz (Department of Chemistry, Umeå University). Abstract Kovachev, P. S. 2018. The role of RNA in prion aggregation and disease. Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology 1620. 81 pp. Uppsala: Acta Universitatis Upsaliensis. ISBN 978-91-513-0208-9. As humanity evolved to witness an exceptionally high standard of living, Alzheimer’s, cancer and diabetes gradually replaced infections as the main limiting factors in longevity. It is both disturbing and captivating that such degenerative conditions are caused by the most ubiquitous biomolecule – the protein. Indeed, proteins are not only the most functional, but also the least understood of the cellular biopolymers. It is then not surprising that many severe human ailments are associated with aberrant proteostasis. The key, causative mechanism of proteinopathy is protein aggregation. Naturally occurring and sometimes functional, aggregation is an auxiliary pathway in protein folding. In the context of a crowded cellular environment, folding and aggregation are the least and one of the least understood molecular processes, respectively. Unravelling one can help deconstruct the other and vice versa, but also can provide mechanistic insight on degenerative proteinopathies. -
Rostaniha 17(2), 2016 115
Archive of SID Ghosta et al. / Study on coprophilous fungi …/ Rostaniha 17(2), 2016 115 DOI: http://dx.doi.org/10.22092/botany.2017.109405 رﺳﺘﻨﯿﻬﺎ Rostaniha 17(2): 115–126 (2016) (1395) 115-126 :(2)17 Study on coprophilous fungi: new records for Iran mycobiota Received: 26.04.2016 / Accepted: 23.10.2016 Youbert Ghosta: Associate Prof. in Plant Pathology, Department of Plant Protection, Urmia University, Urmia, Iran ([email protected]) Alireza Poursafar: Researcher, Department of Plant Protection, College of Agriculture and Natural Resources, University of Tehran, Karaj, Iran Jafar Fathi Qarachal: Researcher, Department of Plant Protection, Urmia University, Urmia, Iran Abstract In a study on coprophilous fungi, different samples including cow, sheep and horse dung and mouse feces were collected from different locations in West and East Azarbaijan provinces (NW Iran). Isolation of the fungi was done based on moist chamber culture method. Purification of the isolated fungi was done by single spore culture method. Several fungal taxa were obtained. Identification of the isolates at species level was done based on morphological characteristics and data obtained from internal transcribed spacer (ITS) regions of ribosomal DNA sequences. In this paper, five taxa viz. Arthrobotrys conoides, Botryosporium longibrachiatum, Cephaliophora irregularis, Oedocephalum glomerulosum, and Podospora pauciseta, all of them belong to Ascomycota, are reported and described. All these taxa are new records for Iran mycobiota. Keywords: Ascomycota, biodiversity, -
Appressorium: the Breakthrough in Dikarya
Journal of Fungi Article Appressorium: The Breakthrough in Dikarya Alexander Demoor, Philippe Silar and Sylvain Brun * Laboratoire Interdisciplinaire des Energies de Demain, LIED-UMR 8236, Université de Paris, 5 rue Marie-Andree Lagroua, 75205 Paris, France * Correspondence: [email protected] Received: 28 May 2019; Accepted: 30 July 2019; Published: 3 August 2019 Abstract: Phytopathogenic and mycorrhizal fungi often penetrate living hosts by using appressoria and related structures. The differentiation of similar structures in saprotrophic fungi to penetrate dead plant biomass has seldom been investigated and has been reported only in the model fungus Podospora anserina. Here, we report on the ability of many saprotrophs from a large range of taxa to produce appressoria on cellophane. Most Ascomycota and Basidiomycota were able to form appressoria. In contrast, none of the three investigated Mucoromycotina was able to differentiate such structures. The ability of filamentous fungi to differentiate appressoria no longer belongs solely to pathogenic or mutualistic fungi, and this raises the question of the evolutionary origin of the appressorium in Eumycetes. Keywords: appressorium; infection cushion; penetration; biomass degradation; saprotrophic fungi; Eumycetes; cellophane 1. Introduction Accessing and degrading biomass are crucial processes for heterotrophic organisms such as fungi. Nowadays, fungi are famous biodegraders that are able to produce an exhaustive set of biomass- degrading enzymes, the Carbohydrate Active enzymes (CAZymes) allowing the potent degradation of complex sugars such as cellulose, hemicellulose, and the more recalcitrant lignin polymer [1]. Because of their importance for industry and biofuel production in particular, many scientific programs worldwide aim at mining this collection of enzymes in fungal genomes and at understanding fungal lignocellulosic plant biomass degradation. -
Molecular Systematics of the Sordariales: the Order and the Family Lasiosphaeriaceae Redefined
Mycologia, 96(2), 2004, pp. 368±387. q 2004 by The Mycological Society of America, Lawrence, KS 66044-8897 Molecular systematics of the Sordariales: the order and the family Lasiosphaeriaceae rede®ned Sabine M. Huhndorf1 other families outside the Sordariales and 22 addi- Botany Department, The Field Museum, 1400 S. Lake tional genera with differing morphologies subse- Shore Drive, Chicago, Illinois 60605-2496 quently are transferred out of the order. Two new Andrew N. Miller orders, Coniochaetales and Chaetosphaeriales, are recognized for the families Coniochaetaceae and Botany Department, The Field Museum, 1400 S. Lake Shore Drive, Chicago, Illinois 60605-2496 Chaetosphaeriaceae respectively. The Boliniaceae is University of Illinois at Chicago, Department of accepted in the Boliniales, and the Nitschkiaceae is Biological Sciences, Chicago, Illinois 60607-7060 accepted in the Coronophorales. Annulatascaceae and Cephalothecaceae are placed in Sordariomyce- Fernando A. FernaÂndez tidae inc. sed., and Batistiaceae is placed in the Euas- Botany Department, The Field Museum, 1400 S. Lake Shore Drive, Chicago, Illinois 60605-2496 comycetes inc. sed. Key words: Annulatascaceae, Batistiaceae, Bolini- aceae, Catabotrydaceae, Cephalothecaceae, Ceratos- Abstract: The Sordariales is a taxonomically diverse tomataceae, Chaetomiaceae, Coniochaetaceae, Hel- group that has contained from seven to 14 families minthosphaeriaceae, LSU nrDNA, Nitschkiaceae, in recent years. The largest family is the Lasiosphaer- Sordariaceae iaceae, which has contained between 33 and 53 gen- era, depending on the chosen classi®cation. To de- termine the af®nities and taxonomic placement of INTRODUCTION the Lasiosphaeriaceae and other families in the Sor- The Sordariales is one of the most taxonomically di- dariales, taxa representing every family in the Sor- verse groups within the Class Sordariomycetes (Phy- dariales and most of the genera in the Lasiosphaeri- lum Ascomycota, Subphylum Pezizomycotina, ®de aceae were targeted for phylogenetic analysis using Eriksson et al 2001).