Lichen Communities on White Oaks in East-Central Illinois

This study was conducted as a survey of epiphytic lichen communities occurring on white oak trees at Walnut Point State Park (Douglas Co.) and Fox Ridge State Park (Coles Co.). Using a system of cover classes to estimate lichen cover, quantitative data on the distribution and abundance of epiphytic lichens was obtained. These data were used to calculate summary statistics of each community including total cover, species richness, and Shannon diversity. A total of ten taxa representing six genera were found. The foliose lichen Physcia millegrana had the highest cover in the open canopy habitats while all other taxa had average coverages of less than one percent. Open canopy habitats had consistantly higher cover than the closed canopy habitats although the Fox Ridge open and closed canopy habitats and the Walnut Point open canopy habitats were similar in species richness and Shannon diversity. The Walnut Point closed canopy habitat was almost completely devoid of lichen cover with only Candelaria concolor occuring on ten percent of white oaks sampled

Lichen Communities on White Oaks in East-Central Illinois

This study was conducted as a survey of epiphytic lichen communities occurring on white oak trees at Walnut Point State Park (Douglas Co.) and Fox Ridge State Park (Coles Co.). Using a system of cover classes to estimate lichen cover, quantitative data on the distribution and abundance of epiphytic lichens was obtained. These data were used to calculate summary statistics of each community including total cover, species richness, and Shannon diversity. A total of ten taxa representing six genera were found. The foliose lichen Physcia millegrana had the highest cover in the open canopy habitats while all other taxa had average coverages of less than one percent. Open canopy habitats had consistantly higher cover than the closed canopy habitats although the Fox Ridge open and closed canopy habitats and the Walnut Point open canopy habitats were similar in species richness and Shannon diversity. The Walnut Point closed canopy habitat was almost completely devoid of lichen cover with only Candelaria concolor occuring on ten percent of white oaks sampled

Novel G-protein-coupled receptor-like proteins in the plant pathogenic fungus Magnaporthe grisea

BACKGROUND: The G-protein-coupled receptors (GPCRs) are one of the largest protein families in human and other animal genomes, but no more than 10 GPCRs have been characterized in fungi. Do fungi contain only this handful or are there more receptors to be discovered? We asked this question using the recently sequenced genome of the fungal plant pathogen Magnaporthe grisea. RESULTS: Proteins with significant similarity to fungus-specific and other eukaryotic GPCRs were identified in M. grisea. These included homologs of known fungal GPCRs, the cAMP receptors from Dictyostelium, and a steroid receptor mPR. We also identified a novel class of receptors typified by PTH11, a cell-surface integral membrane protein required for pathogenicity. PTH11 has seven transmembrane regions and an amino-terminal extracellular cysteine-rich EGF-like domain (CFEM domain), a characteristic also seen in human GPCRs. Sixty-one PTH11-related proteins were identified in M. grisea that shared a common domain with homologs in Neurospora crassa and other fungi belonging to this subphylum of the Ascomycota (the Pezizomycotina). None was detected in other fungal groups (Basidiomycota or other Ascomycota subphyla, including yeasts) or any other eukaryote. The subclass of PTH11 containing the CFEM domain is highly represented in M. grisea. CONCLUSION: In M. grisea we identified homologs of known GPCRs and a novel class of GPCR-like receptors specific to filamentous ascomycetes. A member of this new class, PTH11, is required for pathogenesis, thus suggesting roles in pathogenicity for other members. The identified classes constitute the largest number of GPCR-like proteins reported in fungi to date

The European CCS Demonstration Project Network — A forum for first movers

AbstractThe European CCS Demonstration Project Network was initiated by the European Commission in 2009. The main objective of the network is to accelerate development of CCS technologies by creating a forum for exchange and dissemination of new knowledge generated by the first large scale CCS plants in Europe. This paper provides an overview and understanding of the activities of the network and the political and theoretical context of their development. The paper focuses on how the Network has been structured to add value to demonstration projects and create vital new channels of information for enabling CCS demonstration and deployment to be advanced worldwide

New insights into the evolution and structure of Colletotrichum plant-like subtilisins (CPLSs)

The Colletotrichum plant-like subtilisins (CPLSs) are a family of proteins found only in species of the phytopathogenic fungus Colletotrichum. CPLSs have high similarity to plant subtilisins and our previous work has shown that they were acquired by an ancient horizontal gene transfer event from plants. The rapid growth of sequence data in public databases enabled us to reexamine the structure and evolution of the CPLSs. A new plant subtilisin structural model aided us in refining the tertiary structure of CPLSs. Also, new information about protein interactions of plant subtilisin has provided new insights into the putative function of CPLSs. The availability of new genome sequences of members of the genus Colletotrichum gave us the opportunity to further validate our hypothesis that the CPLSs are unique to the Colletotrichum lineage. Together, this information furthers our knowledge of the potential role of the CPLSs in pathogenicity and the role of HGT in the genome evolution of plant pathogenic fungi.Fil: Armijos Jaramillo, Vinicio. Universidad de Salamanca; EspañaFil: Vargas, Walter Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad de Salamanca; EspañaFil: Sukno, Serenella A.. Universidad de Salamanca; EspañaFil: Thon, Michael R.. Universidad de Salamanca; Españ

New insights into the evolution and structure of Colletotrichum plant-like subtilisins (CPLSs)

The Colletotrichum plant-like subtilisins (CPLSs) are a family of proteins found only in species of the phytopathogenic fungus Colletotrichum. CPLSs have high similarity to plant subtilisins and our previous work has shown that they were acquired by an ancient horizontal gene transfer event from plants. The rapid growth of sequence data in public databases enabled us to reexamine the structure and evolution of the CPLSs. A new plant subtilisin structural model aided us in refining the tertiary structure of CPLSs. Also, new information about protein interactions of plant subtilisin has provided new insights into the putative function of CPLSs. The availability of new genome sequences of members of the genus Colletotrichum gave us the opportunity to further validate our hypothesis that the CPLSs are unique to the Colletotrichum lineage. Together, this information furthers our knowledge of the potential role of the CPLSs in pathogenicity and the role of HGT in the genome evolution of plant pathogenic fungi.Fil: Armijos Jaramillo, Vinicio. Universidad de Salamanca; EspañaFil: Vargas, Walter Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad de Salamanca; EspañaFil: Sukno, Serenella A.. Universidad de Salamanca; EspañaFil: Thon, Michael R.. Universidad de Salamanca; Españ

Concerted action of the Ubiquitin-Fusion Degradation Protein 1 (Ufd1) and Sumo-Targeted Ubiquitin Ligases (STUbLs) in the DNA-damage response

In eukaryotes many players in the DNA-damage response (DDR) catalyze protein sumoylation or ubiquitylation. Emphasis has been placed on how these modifications orchestrate the sequential recruitment of repair factors to sites of DNA damage or stalled replication forks. Here, we shed light on a pathway in which sumoylated factors are eliminated through the coupled action of Sumo-targeted ubiquitin ligases (STUbLs) and the ubiquitin-fusion degradation protein 1 (Ufd1). Ufd1 is a subunit of the Cdc48-Ufd1-Npl4 complex implicated in the sorting of ubiquitylated substrates for degradation by the proteasome. We find that in fission yeast, Ufd1 interacts physically and functionally with the Sumo-targeted ubiquitin ligase (STUbL) Rfp1, homologous to human RNF4, and with the Sumo E3 ligase Pli1, homologous to human PIAS1. Deleting a C-terminal domain of Ufd1 that mediates the interaction of Ufd1 with Rfp1, Pli1, and Sumo (ufd1ΔCt (213-342)) lead to an accumulation of high-molecular-weight Sumo conjugates and caused severe genomic instabilities. The spectrum of sensitivity of ufd1ΔCt (213-342) cells to genotoxins, the epistatic relationships of ufd1ΔCt (213-342) with mutations in DNA repair factors, and the localization of the repair factor Rad22 in ufd1ΔCt (213-342) cells point to ufd1ΔCt (213-342) cells accumulating aberrant structures during replication that require homologous recombination (HR) for their repair. We present evidence that HR is however often not successful in ufd1ΔCt (213-342) cells and we identify Rad22 as one of the high-molecular-weight conjugates accumulating in the ufd1ΔCt (213-342) mutant consistent with Rad22 being a STUbL/Ufd1 substrate. Suggesting a direct role of Ufd1 in the processing of Sumo-conjugates, Ufd1 formed nuclear foci colocalizing with Sumo during the DDR, and Sumo-conjugates accumulated in foci in the ufd1ΔCt (213-342) mutant. Broader functional relationships between Ufd1 and STUbLs conceivably affect numerous cellular processes beyond the DDR

PoGO: Prediction of Gene Ontology terms for fungal proteins

BACKGROUND: Automated protein function prediction methods are the only practical approach for assigning functions to genes obtained from model organisms. Many of the previously reported function annotation methods are of limited utility for fungal protein annotation. They are often trained only to one species, are not available for high-volume data processing, or require the use of data derived by experiments such as microarray analysis. To meet the increasing need for high throughput, automated annotation of fungal genomes, we have developed a tool for annotating fungal protein sequences with terms from the Gene Ontology. RESULTS: We describe a classifier called PoGO (Prediction of Gene Ontology terms) that uses statistical pattern recognition methods to assign Gene Ontology (GO) terms to proteins from filamentous fungi. PoGO is organized as a meta-classifier in which each evidence source (sequence similarity, protein domains, protein structure and biochemical properties) is used to train independent base-level classifiers. The outputs of the base classifiers are used to train a meta-classifier, which provides the final assignment of GO terms. An independent classifier is trained for each GO term, making the system amenable to updating, without having to re-train the whole system. The resulting system is robust. It provides better accuracy and can assign GO terms to a higher percentage of unannotated protein sequences than other methods that we tested. CONCLUSIONS: Our annotation system overcomes many of the shortcomings that we found in other methods. We also provide a web server where users can submit protein sequences to be annotated