Magallanes foreland basin, Chile and Argentina, 51°30 Kinematic evolution of the Patagonian retroarc fold-and-thrust belt and Email alerting services articles cite this article to receive free e-mail alerts when new www.gsapubs.org/cgi/alerts click Subscribe America Bulletin to subscribe to Geological Society of www.gsapubs.org/subscriptions/ click Permission request to contact GSA http://www.geosociety.org/pubs/copyrt.htm#gsa click official positions of the Society. citizenship, gender, religion, or political viewpoint. Opinions presented in this publication do not reflect presentation of diverse opinions and positions by scientists worldwide, regardless of their race, includes a reference to the article's full citation. GSA provides this and other forums for the the abstracts only of their articles on their own or their organization's Web site providing the posting to further education and science. This file may not be posted to any Web site, but authors may post works and to make unlimited copies of items in GSA's journals for noncommercial use in classrooms requests to GSA, to use a single figure, a single table, and/or a brief paragraph of text in subsequent their employment. Individual scientists are hereby granted permission, without fees or further

Species of Scedosporium and Lomentospora are considered as emerging opportunists, affecting immunosuppressed and otherwise debilitated patients, although classically they are known from causing trauma-associated infections in healthy individuals. Clinical manifestations range from local infection to pulmonary colonization and severe invasive disease, in which mortality rates may be over 80%. These unacceptably high rates are due to the clinical status of patients, diagnostic difficulties, and to intrinsic antifungal resistance of these fungi. In consequence, several consortia have been founded to increase research efforts on these orphan fungi. The current review presents recent findings and summarizes the most relevant points, including the Scedosporium/Lomentospora taxonomy, environmental distribution, epidemiology, pathology, virulence factors, immunology, diagnostic methods, and therapeutic strategies.

Proline residues provide a backbone switch in a polypeptide chain, which is controlled by the cis/trans isomerization about the peptidyl-prolyl bond. Phosphorylation of serine- and threonine-proline motifs has been shown to be a critical regulatory event for many proteins. The biological significance of these motifs has been further highlighted by the discovery of a novel and essential peptidyl-prolyl cis/trans isomerase Pin1. Pin1 is required for progression through mitosis via catalyzing the isomerization of phosphorylated Ser/Thr-Pro motifs specifically present in mitosis-specific phosphoproteins. However, little is known whether the phosphorylation regulates the conformational switch of the Ser/Thr-Pro bonds. Here, we report the synthesis and conformational characterization of a series of peptides that contain the phosphorylated or nonphosphorylated Ser/Thr-Pro motifs. Phosphorylation affected the rate of the cis to trans isomerization of the Thr/Ser-Pro bonds. As determined by a protease-coupled assay, the isomerization rate of phosphorylated Thr-Pro bond was found to be 8-fold slower than that of the nonphosphorylated analogue. Furthermore, studies of the pH dependence of the isomerization of the phosphopeptides reveal that both cis content and the rate constant of prolyl cis to trans isomerization are lower for the dianionic state of the phosphothreonine-containing peptides. These effects of phosphorylation are specific for phosphorylated Ser/Thr since neither phosphorylated Tyr nor glutamic acid was able to affect the prolyl isomerization. Finally, our experiments provide evidence that effective catalysis of cis/trans isomerization of phosphorylated Ser/Thr-Pro bonds by Pin1 is specific to the dianionic form of the substrate. Thus, our results demonstrate that protein phosphorylation specifically regulates the backbone dynamics of the Ser/Thr-Pro motifs and that Pin1 specifically isomerizes the certain conformation of the phosphorylated Ser/Thr-Pro motifs.

The ubiquitin proteasome pathway in plants has been shown to be important for many developmental processes. The E3 ubiquitin-protein ligases facilitate transfer of the ubiquitin moiety to substrate proteins. Many E3 ligases contain cullin proteins as core subunits. Here, we show that Arabidopsis (Arabidopsis thaliana) AtCUL3 proteins interact in yeast two-hybrid and in vitro pull-down assays with proteins containing a BTB/POZ (broad complex, tramtrack, bric-a-brac/pox virus and zinc finger) motif. By changing specific amino acid residues within the proteins, critical parts of the cullin and BTB/POZ proteins are defined that are required for these kinds of interactions. In addition, we show that AtCUL3 proteins assemble with the RINGfinger protein AtRBX1 and are targets for the RUB-conjugation pathway. The analysis of AtCUL3a and AtCUL3b expression as well as several BTB/POZ-MATH genes indicates that these genes are expressed in all parts of the plant. The results presented here provide strong evidence that AtCUL3a and AtCUL3b can assemble in Arabidopsis with BTB/POZ-MATH and AtRBX1 proteins to form functional E3 ligases.The ubiquitin proteasome pathway participates in a broad variety of physiologically and developmentally controlled processes in plants (for an overview, see Smalle and Vierstra, 2004). A critical step involves E3 ubiquitin ligases that facilitate the transfer of ubiquitin moieties to a substrate protein, leading to degradation via the 26S proteasome.In Arabidopsis (Arabidopsis thaliana), the bestcharacterized E3s are the SCF (Skp1-cullin-F-box) complexes that consist of at least four subunits: a cullin protein (AtCUL1), an ASK (Arabidopsis Skp1 ortholog) protein, a RING finger protein (RBX1), and an F-box protein (Gray et al., 1999Lechner et al., 2002;Shen et al., 2002). The cullin is a scaffolding subunit for the SCF and binds the ASK-F-box and RBX1 subunits within NH 2 -and COOH-terminal domains, respectively (Zheng et al., 2002). F-box proteins are substrate adaptors that confer specificity to the assembled SCF complexes (Gagne et al., 2002). AtCUL1-dependent E3s are crucial regulators for phytohormone responses, flowering, embryo development, and other processes (Smalle and Vierstra, 2004).At least 11 cullins are encoded in the Arabidopsis genome . However, only six members contain the conserved RUB (related to ubiquitin)-modification site characteristic of cullins that assemble into an SCF or related E3 complex (del Querido et al., 2001;del Pozo et al., 2002). Based on homology to cullins in other organisms, these six Arabidopsis cullins can be classified into three groups. The first group is the CUL1 family, which includes AtCUL1 (At4g02570), AtCUL2 (At1g02980), and AtCUL5 (At1g43140). It is likely that all three members participate in an SCF complex Risseeuw et al., 2003). The second group comprises the CUL3 family with AtCUL3a (At1g26830) and AtCUL3b (At1g69670). These two cullins are approximately 88% identical to each other and represent potential Arabidopsis orthologs of Caenorhabditis...

SummaryCullins are central scaffolding subunits in eukaryotic E3 ligases that facilitate the ubiquitination of target proteins. Arabidopsis contains at least 11 cullin proteins but only a few of them have been assigned biological roles. In this work Arabidopsis cullin 4 is shown to assemble with DDB1, RBX1, DET1 and DDB2 in vitro and in planta. In addition, by using T-DNA insertion and CUL4 antisense lines we demonstrate that corresponding mutants are severely affected in different aspects of development. Reduced CUL4 expression leads to a reduced number of lateral roots, and to abnormal vascular tissue and stomatal development. Furthermore, cul4 mutants display a weak constitutive photomorphogenic phenotype. These results therefore assign an important function to CUL4 during plant development and provide strong evidence that CUL4 assembles together with RBX1 and DDB1 proteins to form a functional E3 ligase in Arabidopsis.

In a genetic screen aimed at the identification of trans-acting factors involved in mRNA 3-end processing of budding yeast, we have previously isolated two temperature-sensitive mutants with an apparent defect in the 3-end formation of a plasmid-derived pre-mRNA. Surprisingly, both mutants were rescued by the essential gene ESS1/PTF1 that encoded a putative peptidylprolyl-cis/trans-isomerase (PPIase) (Hani, J., Stumpf, G., and Domdey, H. (1995) FEBS Lett. 365, 198 -202). Such enzymes, which catalyze the cis/trans-interconversion of peptide bonds N-terminal of prolines, are suggested to play a role in protein folding or trafficking. Here we report that Ptf1p shows PPIase activity in vitro, displaying an unusual substrate specificity for peptides with phosphorylated serine and threonine residues preceding proline. Both mutations were found to result in amino acid substitutions of highly conserved residues within the PPIase domain, causing a marked decrease in PPIase activity of the mutant enzymes. Our results are suggestive of a so far unknown involvement of a PPIase in mRNA 3-end formation in Saccharomyces cerevisiae.Despite intensive efforts to unravel the complex process of mRNA 3Ј-end formation in Saccharomyces cerevisiae, the list of participating factors still awaits its completion.We have recently isolated a gene complementing the phenotype of two temperature-sensitive yeast mutants that were impaired in mRNA 3Ј-end formation. This gene, designated PTF1 (processing/termination factor 1; identical with the previously described ESS1 (1)), encodes a protein that, by virtue of sequence similarity, was identified as a peptidylprolyl-cis/ trans-isomerase (PPIase) 1 (2). PPIases are ubiquitous enzymes that catalyze the interconversion from cis to trans of peptide bonds preceding a proline and are thought to accelerate this often rate-limiting step in the folding of a number of proteins in vivo (3-6).PPIases are divided in three families, based on their sensitivities toward two clinically relevant immunosuppressants: the cyclosporin A-binding proteins (cyclophilins), the FK506-binding proteins, and a third family, named after the Escherichia coli protein parvulin, which is not inhibited by either of the two drugs (for review see Refs. 3-6). In addition, the members of each family are characterized by conserved but distinct amino acid domains. By this criterion, PTF1 was predicted to belong to the parvulin family of PPIases (2).Although disruption of PPIase genes did not generally impair cell growth (7-8), PTF1 was the first PPIase gene shown to be essential for cell viability (1). In fact, PTF1 is the only essential PPIase gene in S. cerevisiae as demonstrated more recently by the viability of a yeast mutant lacking the remaining 12 PPIases, members of the other two immunosuppressant binding families. (8). So far, the only other example of an essential PPIase is the recently discovered PIN1, a human protein, that is structurally and functionally related to Ptf1p (9 -10).In this paper we describe the genetic screen ...

Vitamin B6 represents a highly important group of compounds ubiquitous in all living organisms. It has been demonstrated to alleviate oxidative stress and in its phosphorylated form participates as a cofactor in >100 biochemical reactions. By means of a genetic approach, we have identified a novel mutant, rsr4-1 (for reduced sugar response), with aberrant root and leaf growth that requires supplementation of vitamin B6 for normal development. Cloning of the mutated gene revealed that rsr4-1 carries a point mutation in a member of the PDX1/SOR1/SNZ (for Pyridoxine biosynthesis protein 1/Singlet oxygen resistant 1/Snooze) family that leads to reduced vitamin B6 content. Consequently, metabolism is broadly altered, mainly affecting amino acid, raffinose, and shikimate contents and trichloroacetic acid cycle constituents. Yeast two-hybrid and pull-down analyses showed that Arabidopsis thaliana PDX1 proteins can form oligomers. Interestingly, the mutant form of PDX1 has severely reduced capability to oligomerize, potentially suggesting that oligomerization is important for function. In summary, our results demonstrate the critical function of the PDX1 protein family for metabolism, whole-plant development, and vitamin B6 biosynthesis in higher plants.

The details of how narrow, orogen‐parallel ocean basins are filled with sediment by large axial submarine channels is important to understand because these depositional systems commonly form in through‐like basins in various tectonic settings. The Magallanes foreland basin is an excellent location to study an orogen‐parallel deep‐marine system. Conglomerate lenses of the Upper Cretaceous Cerro Toro Formation have been previously interpreted to represent the fill of a single submarine channel (4–8 km wide, >100 km long) that funneled coarse detritus southward along the basin axis. This interpretation was based on lithologic correlations. New U/Pb dating of zircons from volcanic ashes and sandstones, coupled with strontium isotope stratigraphy, refine the controls on depositional ages and provenance. Results demonstrate that north‐south oriented conglomerate lenses are contemporaneous within error limits (ca. 84–82 Ma) supporting that they represent parts of an axial channel belt. Channel deposits 20 km west of the axial location are 87–82 Ma in age. These channels are partly contemporaneous with the ones within the axial channel belt, making it likely that they represent feeders to the axial channel system. The northern Cerro Toro Formation spans a Turonian to Campanian interval (ca. 90–82 Ma) whereas the formation top, 70 km to the south, is as young as ca. 76 Ma. Kolmogorov–Smirnoff statistical analysis on detrital zircon age distributions shows that the northern uppermost Cerro Toro Formation yields a statistically different age distribution than other samples from the same formation but shows no difference relative to the overlying Tres Pasos Formation. These results suggest the partly coeval deposition of both formations. Integration of previously acquired geochronologic and stratigraphic data with new data show a pronounced southward younging pattern in all four marine formations in the Magallanes Basin. Highly diachronous infilling may be an important depositional pattern for narrow, orogen‐parallel ocean basins.