Grynberg M

References (4)

Title : Comparative genomic analysis of human fungal pathogens causing paracoccidioidomycosis - Desjardins_2011_PLoS.Genet_7_e1002345
Author(s) : Desjardins CA , Champion MD , Holder JW , Muszewska A , Goldberg J , Bailao AM , Brigido MM , Ferreira ME , Garcia AM , Grynberg M , Gujja S , Heiman DI , Henn MR , Kodira CD , Leon-Narvaez H , Longo LV , Ma LJ , Malavazi I , Matsuo AL , Morais FV , Pereira M , Rodriguez-Brito S , Sakthikumar S , Salem-Izacc SM , Sykes SM , Teixeira MM , Vallejo MC , Walter ME , Yandava C , Young S , Zeng Q , Zucker J , Felipe MS , Goldman GH , Haas BJ , McEwen JG , Nino-Vega G , Puccia R , San-Blas G , Soares CMF , Birren BW , Cuomo CA
Ref : PLoS Genet , 7 :e1002345 , 2011
Abstract : Paracoccidioides is a fungal pathogen and the cause of paracoccidioidomycosis, a health-threatening human systemic mycosis endemic to Latin America. Infection by Paracoccidioides, a dimorphic fungus in the order Onygenales, is coupled with a thermally regulated transition from a soil-dwelling filamentous form to a yeast-like pathogenic form. To better understand the genetic basis of growth and pathogenicity in Paracoccidioides, we sequenced the genomes of two strains of Paracoccidioides brasiliensis (Pb03 and Pb18) and one strain of Paracoccidioides lutzii (Pb01). These genomes range in size from 29.1 Mb to 32.9 Mb and encode 7,610 to 8,130 genes. To enable genetic studies, we mapped 94% of the P. brasiliensis Pb18 assembly onto five chromosomes. We characterized gene family content across Onygenales and related fungi, and within Paracoccidioides we found expansions of the fungal-specific kinase family FunK1. Additionally, the Onygenales have lost many genes involved in carbohydrate metabolism and fewer genes involved in protein metabolism, resulting in a higher ratio of proteases to carbohydrate active enzymes in the Onygenales than their relatives. To determine if gene content correlated with growth on different substrates, we screened the non-pathogenic onygenale Uncinocarpus reesii, which has orthologs for 91% of Paracoccidioides metabolic genes, for growth on 190 carbon sources. U. reesii showed growth on a limited range of carbohydrates, primarily basic plant sugars and cell wall components; this suggests that Onygenales, including dimorphic fungi, can degrade cellulosic plant material in the soil. In addition, U. reesii grew on gelatin and a wide range of dipeptides and amino acids, indicating a preference for proteinaceous growth substrates over carbohydrates, which may enable these fungi to also degrade animal biomass. These capabilities for degrading plant and animal substrates suggest a duality in lifestyle that could enable pathogenic species of Onygenales to transfer from soil to animal hosts.
ESTHER : Desjardins_2011_PLoS.Genet_7_e1002345
PubMedSearch : Desjardins_2011_PLoS.Genet_7_e1002345
PubMedID: 22046142
Gene_locus related to this paper: parbd-c1gc95 , parbp-c0s0d7 , parbp-c0s257 , parbd-c1g8z9 , parba-c1grf0 , parbp-c0s816 , parbp-c0s5g4 , parbd-c1g5f5 , parbd-c1fzf9 , parba-kex1 , parbd-kex1 , parbp-kex1 , parba-cbpya , parbp-cbpya

Title : Comparative genomic analyses of the human fungal pathogens Coccidioides and their relatives - Sharpton_2009_Genome.Res_19_1722
Author(s) : Sharpton TJ , Stajich JE , Rounsley SD , Gardner MJ , Wortman JR , Jordar VS , Maiti R , Kodira CD , Neafsey DE , Zeng Q , Hung CY , McMahan C , Muszewska A , Grynberg M , Mandel MA , Kellner EM , Barker BM , Galgiani JN , Orbach MJ , Kirkland TN , Cole GT , Henn MR , Birren BW , Taylor JW
Ref : Genome Res , 19 :1722 , 2009
Abstract : While most Ascomycetes tend to associate principally with plants, the dimorphic fungi Coccidioides immitis and Coccidioides posadasii are primary pathogens of immunocompetent mammals, including humans. Infection results from environmental exposure to Coccidiodies, which is believed to grow as a soil saprophyte in arid deserts. To investigate hypotheses about the life history and evolution of Coccidioides, the genomes of several Onygenales, including C. immitis and C. posadasii; a close, nonpathogenic relative, Uncinocarpus reesii; and a more diverged pathogenic fungus, Histoplasma capsulatum, were sequenced and compared with those of 13 more distantly related Ascomycetes. This analysis identified increases and decreases in gene family size associated with a host/substrate shift from plants to animals in the Onygenales. In addition, comparison among Onygenales genomes revealed evolutionary changes in Coccidioides that may underlie its infectious phenotype, the identification of which may facilitate improved treatment and prevention of coccidioidomycosis. Overall, the results suggest that Coccidioides species are not soil saprophytes, but that they have evolved to remain associated with their dead animal hosts in soil, and that Coccidioides metabolism genes, membrane-related proteins, and putatively antigenic compounds have evolved in response to interaction with an animal host.
ESTHER : Sharpton_2009_Genome.Res_19_1722
PubMedSearch : Sharpton_2009_Genome.Res_19_1722
PubMedID: 19717792
Gene_locus related to this paper: ajecg-c0nbn5 , ajecg-c0nbz4 , ajecg-c0ndw0 , ajecg-c0nqc6 , ajecg-c0nst6 , ajecg-c0ntx5 , ajecg-c0nu33 , ajecg-c0nzh6 , ajecg-c0p0h0 , ajech-c6h1y9 , ajecn-a6qs62 , ajecn-a6quy7 , ajecn-a6r2c0 , ajecn-a6r491 , ajecn-a6r635 , ajecn-a6rab7 , ajecn-a6ram0 , ajecn-a6rf08 , ajecn-a6rf70 , ajecn-atg15 , ajecn-dapb , ajeds-c5jqx1 , cocim-atg15 , cocim-bst1 , cocim-j3k8a1 , cocp7-c5p0f2 , cocp7-c5p0i6 , cocp7-c5p1s3 , cocp7-c5p1u2 , cocp7-c5p2u8 , cocp7-c5p4s8 , cocp7-c5p4z1 , cocp7-c5p5s7 , cocp7-c5p129 , cocp7-c5p172 , cocp7-c5p250 , cocps-e9ctz7 , cocp7-c5pae0 , cocp7-c5pby4 , cocp7-c5pdn8 , cocp7-c5pdv9 , cocp7-c5pe69 , cocp7-c5pf68 , cocp7-c5pgk6 , cocp7-c5pid0 , cocp7-dapb , cocps-e9cz73 , cocps-e9dbi4 , cocps-e9dbu0 , cocps-e9dfh7 , uncre-c4jf72 , uncre-c4jf79 , uncre-c4ji27 , uncre-c4jj62 , uncre-c4jjs9 , uncre-c4jk71 , uncre-c4jlm9 , uncre-c4jlp5 , uncre-c4jlr7 , uncre-c4jnk2 , uncre-c4jnn3 , uncre-c4juj6 , uncre-c4jve9 , uncre-c4jvh5 , uncre-c4jw09 , uncre-c4jyw9 , uncre-c4jzs5 , uncre-dapb , ajech-c6h9r4 , uncre-c4jds5 , cocp7-c5pii3 , ajecn-a6r5v8 , cocim-j3ka92 , cocp7-c5phc6 , ajecn-a6qtc4 , ajecn-a6r145 , cocps-e9d3i4 , cocp7-c5p7x1 , cocps-e9csw0 , ajecg-c0nww6 , ajecn-kex1 , uncre-kex1 , uncre-cbpya , cocps-kex1 , ajecn-cbpya

Title : The Aspergillus nidulans metE gene is regulated by a second system independent from sulphur metabolite repression - Grynberg_2001_Biochim.Biophys.Acta_1519_78
Author(s) : Grynberg M , Piotrowska M , Pizzinini E , Turner G , Paszewski A
Ref : Biochimica & Biophysica Acta , 1519 :78 , 2001
Abstract : Mutations in the Aspergillus nidulans metE gene lead to requirement for O-acetylhomoserine. The gene was cloned by complementation of the metE31 mutation. The coding sequence was found to be interrupted by two introns of 66 and 50 bp, respectively. metE codes for a peptide of 489 amino acids which belongs to the family of homoserine O-acetyltransferases and a well-defined superfamily of alpha/beta hydrolases. Transcription of the metE gene is strongly up-regulated by a severe limitation of methionine, but not of cysteine. This gene is the first sulphur metabolism gene described in A. nidulans which is not regulated by the sulphur metabolite repression system in which cysteine acts as the low-molecular-weight effector.
ESTHER : Grynberg_2001_Biochim.Biophys.Acta_1519_78
PubMedSearch : Grynberg_2001_Biochim.Biophys.Acta_1519_78
PubMedID: 11406274
Gene_locus related to this paper: emeni-met2

Title : The Aspergillus nidulans cysA gene encodes a novel type of serine O-acetyltransferase which is homologous to homoserine O-acetyltransferases - Grynberg_2000_Microbiology_146 ( Pt 10)_2695
Author(s) : Grynberg M , Topczewski J , Godzik A , Paszewski A
Ref : Microbiology , 146 ( Pt 10) :2695 , 2000
Abstract : The Aspergillus nidulans cysA gene was cloned by functional complementation of the cysA1 mutation that impairs the synthesis of O:-acetylserine. The molecular nature of cysA1 and cysA103 alleles was characterized; a nucleotide substitution and a frame shift were found in the former and a deletion mutation in the latter. The CYSA protein is 525 amino acids long and is encoded by an uninterrupted open reading frame. Expression of the cysA gene appears not to be regulated by sulfur, carbon and nitrogen sources. Protein sequence analysis reveals extensive similarity to homoserine O:-acetyltransferases, particularly the bacterial ones, and no homology with known serine O:-acetyltransferases. The authors propose that the CYSA protein is analogous to serine O:-acetyltransferases, i.e. it catalyses the same reaction but has an independent evolutionary origin.
ESTHER : Grynberg_2000_Microbiology_146 ( Pt 10)_2695
PubMedSearch : Grynberg_2000_Microbiology_146 ( Pt 10)_2695
PubMedID: 11021945
Gene_locus related to this paper: emeni-CYSC