Mitefauna (Arachnida: Acari) associated to grapevine, Vitis vinifera L. (Vitaceae), in the municipalities of Bento Gonçalves and Candiota, Rio Grande do Sul, Brazil.

The mitefauna associated to Merlot and Chardonnay grapevine cultivars and associated plants in the municipalities of Bento Gonçalves and Candiota, Rio Grande do Sul was investigated. The study was developed between October 2006 and September 2007, where 20 grapevine plants were randomly chosen from each municipality and monthly sampled. Three leaves of each plant were taken. A total of 11,598 mites belonging to 14 families and to 52 species were found. Fifty-nine percent of the total specimens were collected in Candiota, being 93% associated to the Merlot cultivar. Higher species richness was observed on associated plants. Phytoseiidae showed the highest species richness, with ten species, and Eriophyidae showed the highest abundance, with 8,675 specimens. Calepitrimerus vitis (Nalepa, 1905) and polyphagotarsonemus latus (Banks, 1904) were the most common phytophagous mites, while Neoseiulus californicus (McGregor, 1954) and Pronematus anconai (Baker, 1943) were the most common predators

Acarofauna (Acari) associada à videira (Vitis vinifera L.) no Estado do Rio Grande do Sul.

Na cultura da videira (Vitis vinifera L.: Vitaceae), ácaros fitófagos das famílias Eriophyidae, Tarsonemidae e Tetranychidae são os mais importantes, enquanto que dentre os predadores destacamse os Phytoseiidae, Stigmaeidae e Iolinidae como inimigos naturais de ácaros praga. O objetivo deste trabalho foi conhecer a acarofauna associada à videira das variedades Alfrocheiro, Cabernet Sauvignon e Pinot Noir, nos municípios de Bento Gonçalves, Candiota e Encruzilhada do Sul, no estado do Rio Grande do Sul. As amostragens foram constituídas de três folhas coletadas de um ramo de 20 plantas tomadas ao acaso em cada área. Para avaliar a presença de ácaros nas gemas, no período de senescência, um ramo foi coletado de cada uma das 20 plantas amostradas. Foram encontrados 57.401 ácaros pertencentes a 18 famílias, 49 gêneros e 69 espécies. Phytoseiidae apresentou maior riqueza, com 17 espécies, seguida por Stigmaeidae, com 10 espécies, e Eriophyidae e Tydeidae, com sete espécies cada. Os Eriophyidae foram mais abundantes, com 88%, seguido de Tetranychidae, com 4% dos ácaros coletados. Calepitrimerus vitis (Nalepa, 1905) e Panonychus ulmi (Koch, 1836) foram os ácaros fitófagos mais comuns e Neoseiulus californicus (McGregor, 1954), Agistemus floridanus Gonzalez, 1965 e Pronematus anconai Baker, (1943) 1944 os ácaros predadores mais comuns. Palavras- Chave: Parreira, Tetranychidae, Phytoseiidae, Iolinidae, Controle biológico

Structure of the first representative of Pfam family PF04016 (DUF364) reveals enolase and Rossmann-like folds that combine to form a unique active site with a possible role in heavy-metal chelation.

The crystal structure of Dhaf4260 from Desulfitobacterium hafniense DCB-2 was determined by single-wavelength anomalous diffraction (SAD) to a resolution of 2.01 Å using the semi-automated high-throughput pipeline of the Joint Center for Structural Genomics (JCSG) as part of the NIGMS Protein Structure Initiative (PSI). This protein structure is the first representative of the PF04016 (DUF364) Pfam family and reveals a novel combination of two well known domains (an enolase N-terminal-like fold followed by a Rossmann-like domain). Structural and bioinformatic analyses reveal partial similarities to Rossmann-like methyltransferases, with residues from the enolase-like fold combining to form a unique active site that is likely to be involved in the condensation or hydrolysis of molecules implicated in the synthesis of flavins, pterins or other siderophores. The genome context of Dhaf4260 and homologs additionally supports a role in heavy-metal chelation

Effects of menstrual phase on intake of nicotine, caffeine, and alcohol and nonprescribed drugs in women with late luteal phase dysphoric disorder

To investigate the possibility that cigarette smoking and other drug use are affected by menstrual phase in smokers with Late Luteal Phase Dysphoric Disorder (LLPDD), we examined daily diaries rating menstrual symptomatology, smoking, alcohol and nonprescription drug use, and caffeine intake in nine female smokers meeting criteria for LLPDD. Menstrual symptomatology peaked during the premenstrual phase. Smoking, alcohol, and nonprescription drug intake were increased during menses; caffeine intake was unaffected by phase. No systematic intrasubject correlation between symptomatology and smoking was detected. It was concluded that in women with LLPDD, smoking and alcohol and nonprescription drug intake appear to vary as a function of menstrual phase. The lack of intrasubject correlations between symptomatology and intake, and the failure of peak intake to coincide with peak symptomatology, however, indicate that these effects cannot be explained simply as "self-medication" of acute episodes of dysphoric mood.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/31910/1/0000863.pd

Structure of a putative NTP pyrophosphohydrolase: YP_001813558.1 from Exiguobacterium sibiricum 255-15.

The crystal structure of a putative NTPase, YP_001813558.1 from Exiguobacterium sibiricum 255-15 (PF09934, DUF2166) was determined to 1.78 Å resolution. YP_001813558.1 and its homologs (dimeric dUTPases, MazG proteins and HisE-encoded phosphoribosyl ATP pyrophosphohydrolases) form a superfamily of all-α-helical NTP pyrophosphatases. In dimeric dUTPase-like proteins, a central four-helix bundle forms the active site. However, in YP_001813558.1, an unexpected intertwined swapping of two of the helices that compose the conserved helix bundle results in a `linked dimer' that has not previously been observed for this family. Interestingly, despite this novel mode of dimerization, the metal-binding site for divalent cations, such as magnesium, that are essential for NTPase activity is still conserved. Furthermore, the active-site residues that are involved in sugar binding of the NTPs are also conserved when compared with other α-helical NTPases, but those that recognize the nucleotide bases are not conserved, suggesting a different substrate specificity

The structure of BVU2987 from Bacteroides vulgatus reveals a superfamily of bacterial periplasmic proteins with possible inhibitory function.

Proteins that contain the DUF2874 domain constitute a new Pfam family PF11396. Members of this family have predominantly been identified in microbes found in the human gut and oral cavity. The crystal structure of one member of this family, BVU2987 from Bacteroides vulgatus, has been determined, revealing a β-lactamase inhibitor protein-like structure with a tandem repeat of domains. Sequence analysis and structural comparisons reveal that BVU2987 and other DUF2874 proteins are related to β-lactamase inhibitor protein, PepSY and SmpA_OmlA proteins and hence are likely to function as inhibitory proteins

Structure of the γ-D-glutamyl-L-diamino acid endopeptidase YkfC from Bacillus cereus in complex with L-Ala-γ-D-Glu: insights into substrate recognition by NlpC/P60 cysteine peptidases.

Dipeptidyl-peptidase VI from Bacillus sphaericus and YkfC from Bacillus subtilis have both previously been characterized as highly specific γ-D-glutamyl-L-diamino acid endopeptidases. The crystal structure of a YkfC ortholog from Bacillus cereus (BcYkfC) at 1.8 Å resolution revealed that it contains two N-terminal bacterial SH3 (SH3b) domains in addition to the C-terminal catalytic NlpC/P60 domain that is ubiquitous in the very large family of cell-wall-related cysteine peptidases. A bound reaction product (L-Ala-γ-D-Glu) enabled the identification of conserved sequence and structural signatures for recognition of L-Ala and γ-D-Glu and, therefore, provides a clear framework for understanding the substrate specificity observed in dipeptidyl-peptidase VI, YkfC and other NlpC/P60 domains in general. The first SH3b domain plays an important role in defining substrate specificity by contributing to the formation of the active site, such that only murein peptides with a free N-terminal alanine are allowed. A conserved tyrosine in the SH3b domain of the YkfC subfamily is correlated with the presence of a conserved acidic residue in the NlpC/P60 domain and both residues interact with the free amine group of the alanine. This structural feature allows the definition of a subfamily of NlpC/P60 enzymes with the same N-terminal substrate requirements, including a previously characterized cyanobacterial L-alanine-γ-D-glutamate endopeptidase that contains the two key components (an NlpC/P60 domain attached to an SH3b domain) for assembly of a YkfC-like active site

Structural and Sequence Analysis of Imelysin-Like Proteins Implicated in Bacterial Iron Uptake

Imelysin-like proteins define a superfamily of bacterial proteins that are likely involved in iron uptake. Members of this superfamily were previously thought to be peptidases and were included in the MEROPS family M75. We determined the first crystal structures of two remotely related, imelysin-like proteins. The Psychrobacter arcticus structure was determined at 2.15 Å resolution and contains the canonical imelysin fold, while higher resolution structures from the gut bacteria Bacteroides ovatus, in two crystal forms (at 1.25 Å and 1.44 Å resolution), have a circularly permuted topology. Both structures are highly similar to each other despite low sequence similarity and circular permutation. The all-helical structure can be divided into two similar four-helix bundle domains. The overall structure and the GxHxxE motif region differ from known HxxE metallopeptidases, suggesting that imelysin-like proteins are not peptidases. A putative functional site is located at the domain interface. We have now organized the known homologous proteins into a superfamily, which can be separated into four families. These families share a similar functional site, but each has family-specific structural and sequence features. These results indicate that imelysin-like proteins have evolved from a common ancestor, and likely have a conserved function

The Center for Eukaryotic Structural Genomics

The Center for Eukaryotic Structural Genomics (CESG) is a “specialized” or “technology development” center supported by the Protein Structure Initiative (PSI). CESG’s mission is to develop improved methods for the high-throughput solution of structures from eukaryotic proteins, with a very strong weighting toward human proteins of biomedical relevance. During the first three years of PSI-2, CESG selected targets representing 601 proteins from Homo sapiens, 33 from mouse, 10 from rat, 139 from Galdieria sulphuraria, 35 from Arabidopsis thaliana, 96 from Cyanidioschyzon merolae, 80 from Plasmodium falciparum, 24 from yeast, and about 25 from other eukaryotes. Notably, 30% of all structures of human proteins solved by the PSI Centers were determined at CESG. Whereas eukaryotic proteins generally are considered to be much more challenging targets than prokaryotic proteins, the technology now in place at CESG yields success rates that are comparable to those of the large production centers that work primarily on prokaryotic proteins. We describe here the technological innovations that underlie CESG’s platforms for bioinformatics and laboratory information management, target selection, protein production, and structure determination by X-ray crystallography or NMR spectroscopy