The radiation of Satyrini butterflies (Nymphalidae: Satyrinae): a challenge for phylogenetic methods

We have inferred the most comprehensive phylogenetic hypothesis to date of butterflies in the tribe Satyrini. In order to obtain a hypothesis of relationships, we used maximum parsimony and model‐based methods with 4435 bp of DNA sequences from mitochondrial and nuclear genes for 179 taxa (130 genera and eight out‐groups). We estimated dates of origin and diversification for major clades, and performed a biogeographic analysis using a dispersal–vicariance framework, in order to infer a scenario of the biogeographical history of the group. We found long‐branch taxa that affected the accuracy of all three methods. Moreover, different methods produced incongruent phylogenies. We found that Satyrini appeared around 42 Mya in either the Neotropical or the Eastern Palaearctic, Oriental, and/or Indo‐Australian regions, and underwent a quick radiation between 32 and 24 Mya, during which time most of its component subtribes originated. Several factors might have been important for the diversification of Satyrini: the ability to feed on grasses; early habitat shift into open, non‐forest habitats; and geographic bridges, which permitted dispersal over marine barriers, enabling the geographic expansions of ancestors to new environments that provided opportunities for geographic differentiation, and diversification.

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A Retroviral Chimeric Capsid Protein Reveals the Role of the N-Terminal β-Hairpin in Mature Core Assembly

The human immunodeficiency virus (HIV) is an enveloped virus constituted by two monomeric RNA molecules that encode for 15 proteins. Among these are the structural proteins that are translated as the gag polyprotein. In order to become infectious, HIV must undergo a maturation process mediated by the proteolytic cleavage of gag to give rise to the isolated structural protein matrix, capsid (CA), nucleocapsid as well as p6 and spacer peptides 1 and 2. Upon maturation, the 13 N-terminal residues from CA fold into a β-hairpin, which is stabilized mainly by a salt bridge between Pro1 and Asp51. Previous reports have shown that non-formation of the salt bridge, which potentially disrupts proper β-hairpin arrangement, generates noninfectious virus or aberrant cores. To date, however, there is no consensus on the role of the β-hairpin. In order to shed light in this subject, we have generated mutations in the hairpin region to examine what features would be crucial for the β-hairpin's role in retroviral mature core formation. These features include the importance of the proline at the N-terminus, the amino acid sequence, and the physical structure of the β-hairpin itself. The presented experiments provide biochemical evidence that β-hairpin formation plays an important role in regard to CA protein conformation required to support proper mature core arrangement. Hydrogen/deuterium exchange and in vitro assembly reactions illustrated the importance of the β-hairpin structure, its dynamics, and its influence on the orientation of helix 1 for the assembly of the mature CA lattice.     

False fairy wasps in Early Cretaceous amber from Spain (Hymenoptera: Mymarommatoidea)

Abstract: The fauna of false fairy wasps (Proctotrupomorpha: Bipetiolarida: Mymarommatoidea) occurring in Early Cretaceous (Albian) amber from north and north‐eastern Spain (Moraza, San Just, and El Soplao outcrops) is described. In total, 12 specimens have been recovered and four species recognized, all new: Alavaromma orchamum gen. nov. and sp. nov. (Alavarommatidae fam. nov.), Archaeromma hispanicum sp. nov. (Mymarommatidae), Galloromma alavaensis sp. nov., and G. turolensis sp. nov. (Gallorommatidae). The study indicates the necessity of revision and maybe fusion of both superfamilies, Mymarommatoidea and Serphitoidea, as the boundaries between them are less and less defined. However, major classificatory rearrangements must await the completion of the cladistic studies presently underway.     

Structural Plasticity of the Protein Plug That Traps Newly Packaged Genomes in Podoviridae Virions

Bacterial viruses of the P22-like family encode a specialized tail needle essential for genome stabilization after DNA packaging and implicated in Gram-negative cell envelope penetration. The atomic structure of P22 tail needle (gp26) crystallized at acidic pH reveals a slender fiber containing an N-terminal “trimer of hairpins” tip. Although the length and composition of tail needles vary significantly in Podoviridae, unexpectedly, the amino acid sequence of the N-terminal tip is exceptionally conserved in more than 200 genomes of P22-like phages and prophages. In this paper, we used x-ray crystallography and EM to investigate the neutral pH structure of three tail needles from bacteriophage P22, HK620, and Sf6. In all cases, we found that the N-terminal tip is poorly structured, in stark contrast to the compact trimer of hairpins seen in gp26 crystallized at acidic pH. Hydrogen-deuterium exchange mass spectrometry, limited proteolysis, circular dichroism spectroscopy, and gel filtration chromatography revealed that the N-terminal tip is highly dynamic in solution and unlikely to adopt a stable trimeric conformation at physiological pH. This is supported by the cryo-EM reconstruction of P22 mature virion tail, where the density of gp26 N-terminal tip is incompatible with a trimer of hairpins. We propose the tail needle N-terminal tip exists in two conformations: a pre-ejection extended conformation, which seals the portal vertex after genome packaging, and a postejection trimer of hairpins, which forms upon its release from the virion. The conformational plasticity of the tail needle N-terminal tip is built in the amino acid sequence, explaining its extraordinary conservation in nature.     

A spectacular new species of Nepenthes L. (Nepenthaceae) pitcher plant from central Palawan,Philippines

A new species of Nepenthes L., N. attenboroughii (Nepenthaceae), from Palawan Island in the Philippines, is described and illustrated. It is restricted to rocky, ultramafic soils that comprise the summit region of Mount Victoria, Municipality of Narra, where it occurs in isolation from other members of the genus. On the basis of the morphological features, this new taxon appears to be related to both N. mira Jebb & Cheek of Palawan and N. rajah Hook.f. of Borneo. Its substantial size places it among the largest of known pitcher plants. The diagnostic morphological characters are discussed and an updated key is provided for a revised complex of Nepenthes species from the Palawan and North Borneo phytogeographical region. © 2009 The Linnean Society of London, Botanical Journal of the Linnean Society, 2009, 159 , 195–202.     

Nucleation and growth phases in the polymerization of coat and scaffolding subunits into icosahedral procapsid shells.

The polymerization of protein subunits into precursor shells empty of DNA is a critical process in the assembly of double-stranded DNA viruses. For the well-characterized icosahedral procapsid of phage P22, coat and scaffolding protein subunits do not assemble separately but, upon mixing, copolymerize into double-shelled procapsids in vitro. The polymerization reaction displays the characteristics of a nucleation limited reaction: a paucity of intermediate assembly states, a critical concentration, and kinetics displaying a lag phase. Partially formed shell intermediates were directly visualized during the growth phase by electron microscopy of the reaction mixture. The morphology of these intermediates suggests that assembly is a highly directed process. The initial rate of this reaction depends on the fifth power of the coat subunit concentration and the second or third power of the scaffolding concentration, suggesting that pentamer of coat protein and dimers or trimers of scaffolding protein, respectively, participate in the rate-limiting step.     

Conformational states of the bacteriophage P22 capsid subunit in relation to self-assembly

The formation of closed icosahedral capsids from a single species of coat protein subunit requires that the subunits assume different conformations at different lattice positions. In the double-stranded DNA bacteriophage P22, formation of correctly dimensioned capsids is mediated by interaction between coat protein subunits and scaffolding protein. Raman spectroscopy has been employed to compare the conformations of coat protein subunits which have been polymerized to form capsids in the presence and absence of the of scaffolding protein display a Raman spectrum characterized by a broad amide I band centered at 1665 cm-1 with a discernible shoulder near 1653 cm-1, and a broad amide III profile centered at 1238 cm-1 but asymmetrically skewed to higher frequency. These spectral features indicate that the protein conformation in procapsid shells is rich in beta-sheet secondary structure but contains also a significant distribution of alpha-helix. When biologically active, purified subunits assemble in the absence of scaffolding protein, they form polydisperse multimers lacking the proper dimensions of procapsid closed shells. We designate these multimers as "associated subunits" (AS). The Raman spectrum of associated subunits indicates a narrower distribution of secondary structure. The associated subunits are characterized by a sharper and more intense Raman amide I band at 1666 cm-1, with no prominent amide I shoulder of lower frequency. An analogous narrowing of the Raman amide III profile is also observed for AS particles, with an accompanying shift of the amide III band center to 1235 cm-1.(ABSTRACT TRUNCATED AT 250 WORDS)     

Cavity defects in the procapsid of bacteriophage P22 and the mechanism of capsid maturation

Bacteriophage P22 belongs to a family of double-stranded DNA viruses that share common morphogenetic features like DNA packaging into a procapsid precursor and maturation. Maturation involves cooperative expansion of the procapsid shell with concomitant lattice stabilization. The expansion is thought to be mediated by movement of two coat protein domains around a hinge. The metastable conformation of subunit within the procapsid lattice is considered to constitute a late folding intermediate. In order to understand the mechanism of expansion it is necessary to characterize the interactions stabilizing procapsid and mature capsid lattices, respectively. We employ pressure dissociation to compare subunit packing within the procapsid and expanded lattice. Procapsid shells contain larger cavities than the expanded shells, presumably due to polypeptide packing defects. These defects contribute to the metastable nature of the procapsid lattice and are cured during expansion. Improved packing contributes to the increased stability of the expanded shell. Comparison of two temperature-sensitive folding (tsf) mutants of coat protein (T294I and W48Q) with wild-type coat revealed that both mutations markedly destabilized the procapsid shell and yet had little effect on relative stability of the monomeric subunit. Thus, the regions affected by these packing defects constitute subunit interfaces of the procapsid shell. The larger activation volume of pressure dissociation observed for both T294I and W48Q indicates that the decreased stability of these particles is due to increase of cavity defects. These defects in the procapsid lattice are cured upon expansion suggesting that the intersubunit contacts affected by tsf mutations are absent or rearranged in the mature shell. The energetics of the in vitro expansion reaction also suggests that entropic stabilization contributes to the large free energy barrier for expansion.     

An improved method using densitometry for evaluating severity of laser photocoagulation induced CNV

Laser photocoagulation induced choroidal neovascularization currently is the most effective model available for the study of this disease in terms of efficacy of new drugs and therapies. Previously, evaluating the extent of choroidal neovascularization using this model was time- consuming and required the use of experienced personnel. We describe a new method for simple and rapid evaluation of laser induced choroidal neovascularization using densitometry. Fluorescein angiograms of a laser photocoagulated rat eye were scanned into a computer. Densitometry software subsequently was used to calculate the severity of the laser lesions. The densitometry method proved effective for calculating the extent of laser induced choroidal neovascularization. In addition, this method was more rapid than visual evaluations and less likely to produce errors.     

Remote estimation of carbon dioxide uptake by a Mediterranean forest

The estimation of the carbon balance in ecosystems, regions, and the biosphere is currently one of the main concerns in the study of the ecology of global change. Current remote sensing methodologies for estimating gross primary productivity are not satisfactory because they rely too heavily on (i) the availability of climatic data, (ii) the definition of land‐use cover, and (iii) the assumptions of the effects of these two factors on the radiation‐use efficiency of vegetation (RUE). A new methodology is urgently needed that will actually assess RUE and overcome the problems associated with the capture of fluctuations in carbon absorption in space and over time. Remote sensing techniques such as the widely used reflectance vegetation indices (e.g. NDVI, EVI) allow green plant biomass and therefore plant photosynthetic capacity to be assessed. However, there are vegetation types, such as the Mediterranean forests, with a very low seasonality of these vegetation indices and a high seasonality of carbon uptake. In these cases it is important to detect how much of this capacity is actually realized, which is a much more challenging goal. The photochemical reflectance index (PRI) derived from freely available satellite information (MODIS sensor) presented for a 5‐year analysis for a Mediterranean forest a positive relationship with the RUE. Thus, we show that it is possible to estimate RUE and GPP in real time and therefore actual carbon uptake of Mediterranean forests at ecosystem level using the PRI. This conceptual and technological advancement would avoid the need to rely on the sometimes unreliable maximum RUE.