Promoting Positive Youth Development Through School-Based Social and Emotional Learning Interventions: A Meta-Analysis of Follow-Up Effects.

This meta-analysis reviewed 82 school-based, universal social and emotional learning (SEL) interventions involving 97,406 kindergarten to high school students (Mage  = 11.09 years; mean percent low socioeconomic status = 41.1; mean percent students of color = 45.9). Thirty-eight interventions took place outside the United States. Follow-up outcomes (collected 6 months to 18 years postintervention) demonstrate SEL's enhancement of positive youth development. Participants fared significantly better than controls in social-emotional skills, attitudes, and indicators of well-being. Benefits were similar regardless of students' race, socioeconomic background, or school location. Postintervention social-emotional skill development was the strongest predictor of well-being at follow-up. Infrequently assessed but notable outcomes (e.g., graduation and safe sexual behaviors) illustrate SEL's improvement of critical aspects of students' developmental trajectories.

Evidence supporting the 19 ß-strand model for Tom40 from cysteine scanning and protease site accessibility studies.

Most proteins found in mitochondria are translated in the cytosol and enter the organelle via the TOM complex (translocase of the outer mitochondrial membrane). Tom40 is the pore forming component of the complex. Although the three-dimensional structure of Tom40 has not been determined, the structure of porin, a related protein, has been shown to be a ß-barrel containing 19 membrane spanning ß-strands and an N-terminal α-helical region. The evolutionary relationship between the two proteins has allowed modeling of Tom40 into a similar structure by several laboratories. However, it has been suggested that the 19-strand porin structure does not represent the native form of the protein. If true, modeling of Tom40 based on the porin structure would also be invalid. We have used substituted cysteine accessibility mapping to identify several potential ß-strands in the Tom40 protein in isolated mitochondria. These data, together with protease accessibility studies, support the 19 ß-strand model for Tom40 with the C-terminal end of the protein localized to the intermembrane space.

The impact of enhancing students' social and emotional learning: a meta-analysis of school-based universal interventions.

This article presents findings from a meta-analysis of 213 school-based, universal social and emotional learning (SEL) programs involving 270,034 kindergarten through high school students. Compared to controls, SEL participants demonstrated significantly improved social and emotional skills, attitudes, behavior, and academic performance that reflected an 11-percentile-point gain in achievement. School teaching staff successfully conducted SEL programs. The use of 4 recommended practices for developing skills and the presence of implementation problems moderated program outcomes. The findings add to the growing empirical evidence regarding the positive impact of SEL programs. Policy makers, educators, and the public can contribute to healthy development of children by supporting the incorporation of evidence-based SEL programming into standard educational practice.

Mitochondrial F1Fo-ATP synthase: the small subunits e and g associate with monomeric complexes to trigger dimerization.

Mitochondrial F(1)F(o)-ATP synthase catalyzes the formation of ATP from ADP and inorganic phosphate. The enzyme is found in monomeric, dimeric and higher oligomeric forms in the inner mitochondrial membrane. Dimerization of ATP synthase complexes is a prerequisite for the generation of larger oligomers that promote membrane bending and formation of tubular cristae membranes. Two small proteins of the membrane-embedded F(o)-domain, subunit e (Su e; Atp21) and Su g (Atp20), were identified as dimer-specific subunits of yeast ATP synthase and shown to be required for stabilization of the dimers. We have identified two distinct monomeric forms of yeast ATP synthase. Su e and Su g are present not only in the dimer but also in one of the monomeric forms. We demonstrate that Su e and Su g sequentially assemble with monomeric ATP synthase to form a dimerization-competent primed monomer. We conclude that association of Su e and Su g with monomeric F(1)F(o)-ATP synthase represents an initial step of oligomer formation.

Vaccine production in Neurospora crassa.

We have chosen to use the filamentous fungus Neurospora crassa to produce subunit vaccines. Here we describe the production and purification of Influenza hemagglutinin and neuraminidase antigens in N. crassa. The N. crassa system used by Neugenesis offers many advantages over other systems for production of recombinant protein. In contrast to mammalian cell culture, N. crassa can be grown in a rapid and economic manner, generating large amounts of recombinant protein in simple, defined medium. Vaccines, therefore, can be produced more rapidly and at lower cost than conventional cell culture or egg-based systems. This has important applications to tailoring the seasonal vaccine supply and responding to new pandemics.

Proteomic analyses of Fusarium graminearum grown under mycotoxin-inducing conditions.

Non-gel-based quantitative proteomics technology was used to profile protein expression differences when Fusarium graminearum was induced to produce trichothecenes in vitro. As F. graminearum synthesizes and secretes trichothecenes early in the cereal host invasion process, we hypothesized that proteins contributing to infection would also be induced under conditions favouring mycotoxin synthesis. Protein samples were extracted from three biological replicates of a time course study and subjected to iTRAQ (isobaric tags for relative and absolute quantification) analysis. Statistical analysis of a filtered dataset of 435 proteins revealed 130 F. graminearum proteins that exhibited significant changes in expression, of which 72 were upregulated relative to their level at the initial phase of the time course. There was good agreement between upregulated proteins identified by 2-D PAGE/MS/MS and iTRAQ. RT-PCR and northern hybridization confirmed that genes encoding proteins which were upregulated based on iTRAQ were also transcriptionally active under mycotoxin producing conditions. Numerous candidate pathogenicity proteins were identified using this technique. These will provide leads in the search for mechanisms and markers of host invasion and novel antifungal targets.

Effects of positive youth development programs on school, family, and community systems.

A review of efforts at social system change in 526 universal competence-promotion outcome studies indicated that 64% of the interventions attempted some type of microsystemic or mesosystemic change involving schools, families, or community-based organizations in an attempt to foster developmental competencies in children and adolescents. Only 24% of the reports provided quantitative data on the change that occurred in targeted systems. However, studies containing the necessary information produced several mean effect sizes that were statistically significant, and ranged from modest to large in magnitude. These data indicate that attempts to change social systems affecting children and adolescents can be successful. Future work should measure more thoroughly the extent to which the systemic changes that are targeted through intervention are achieved, and investigate how such changes contribute to the development and sustainability of the outcomes that might be demonstrated by participants of competence-promotion programs.

Effect of mutations in Tom40 on stability of the translocase of the outer mitochondrial membrane (TOM) complex, assembly of Tom40, and import of mitochondrial preproteins.

Mitochondrial preproteins synthesized in the cytosol are imported through the mitochondrial outer membrane by the translocase of the outer mitochondrial membrane (TOM) complex. Tom40 is the major component of the complex and is essential for cell viability. We generated 21 different mutations in conserved regions of the Neurospora crassa Tom40 protein. The mutant genes were transformed into a tom40 null nucleus maintained in a sheltered heterokaryon, and 17 of the mutant genes gave rise to viable strains. All mutations reduced the efficiency of the altered Tom40 molecules to assemble into the TOM complex. Mitochondria isolated from seven of the mutant strains had defects for importing mitochondrial preproteins. Only one strain had a general import defect for all preproteins examined. Another mutation resulted in defects in the import of a matrix-destined preprotein and an outer membrane beta-barrel protein, but import of the ADP/ATP carrier to the inner membrane was unaffected. Five strains showed deficiencies in the import of beta-barrel proteins. The latter results suggest that the TOM complex distinguishes beta-barrel proteins from other classes of preprotein during import. This supports the idea that the TOM complex plays an active role in the transfer of preproteins to subsequent translocases for insertion into the correct mitochondrial subcompartment.

Mdm38 interacts with ribosomes and is a component of the mitochondrial protein export machinery.

Saccharomyces cerevisiae Mdm38 and Ylh47 are homologues of human Letm1, a protein implicated in Wolf-Hirschhorn syndrome. We analyzed the function of Mdm38 and Ylh47 in yeast mitochondria to gain insight into the role of Letm1. We find that mdm38Delta mitochondria have reduced amounts of certain mitochondrially encoded proteins and low levels of complex III and IV and accumulate unassembled Atp6 of complex V of the respiratory chain. Mdm38 is especially required for efficient transport of Atp6 and cytochrome b across the inner membrane, whereas Ylh47 plays a minor role in this process. Both Mdm38 and Ylh47 form stable complexes with mitochondrial ribosomes, similar to what has been reported for Oxa1, a central component of the mitochondrial export machinery. Our results indicate that Mdm38 functions as a component of an Oxa1-independent insertion machinery in the inner membrane and that Mdm38 plays a critical role in the biogenesis of the respiratory chain by coupling ribosome function to protein transport across the inner membrane.

Taz1, an outer mitochondrial membrane protein, affects stability and assembly of inner membrane protein complexes: implications for Barth Syndrome.

The Saccharomyces cerevisiae Taz1 protein is the orthologue of human Tafazzin, a protein that when inactive causes Barth Syndrome (BTHS), a severe inherited X-linked disease. Taz1 is a mitochondrial acyltransferase involved in the remodeling of cardiolipin. We show that Taz1 is an outer mitochondrial membrane protein exposed to the intermembrane space (IMS). Transport of Taz1 into mitochondria depends on the receptor Tom5 of the translocase of the outer membrane (TOM complex) and the small Tim proteins of the IMS, but is independent of the sorting and assembly complex (SAM). TAZ1 deletion in yeast leads to growth defects on nonfermentable carbon sources, indicative of a defect in respiration. Because cardiolipin has been proposed to stabilize supercomplexes of the respiratory chain complexes III and IV, we assess supercomplexes in taz1delta mitochondria and show that these are destabilized in taz1Delta mitochondria. This leads to a selective release of a complex IV monomer from the III2IV2 supercomplex. In addition, assembly analyses of newly imported subunits into complex IV show that incorporation of the complex IV monomer into supercomplexes is affected in taz1Delta mitochondria. We conclude that inactivation of Taz1 affects both assembly and stability of respiratory chain complexes in the inner membrane of mitochondria.

The protein import and assembly machinery of the mitochondrial outer membrane.

The process of mitochondrial protein import has been studied for many years. Despite this attention, many processes associated with mitochondrial biogenesis are poorly understood. Insight into one of these processes, assembly of beta-barrel proteins into the mitochondrial outer membrane, will be discussed. This review focuses on recent data that suggest that assembly of beta-barrel proteins into the outer mitochondrial membrane is dependent on a newly identified protein complex termed the sorting and assembly machinery (SAM complex). Members of the SAM complex have been identified in both eukaryotic and prokaryotic organisms, suggesting that the process of beta-barrel assembly into membranes has been conserved through evolution.

Characterization of Neurospora crassa Tom40-deficient mutants and effect of specific mutations on Tom40 assembly.

The TOM complex (Translocase of the Outer mitochondrial Membrane) is responsible for the recognition of mitochondrial preproteins synthesized in the cytosol and for their translocation across or into the outer mitochondrial membrane. Tom40 is the major component of the TOM complex and forms the translocation pore. We have created a tom40 mutant of Neurospora crassa and have demonstrated that the gene is essential for the viability of the organism. Mitochondria with reduced levels of Tom40 were deficient for import of mitochondrial preproteins and contained reduced levels of the TOM complex components Tom22 and Tom6, suggesting that the import and/or stability of these proteins is dependent on the presence of Tom40. Mutant Tom40 preproteins were analyzed for their ability to be assembled into the TOM complex. In vitro import assays revealed that conserved regions near the N terminus (residues 51-60) and the C terminus (residues 321-323) of the 349-amino acid protein were required for assembly beyond a 250-kDa intermediate form. Mutant strains expressing Tom40 with residues 51-60 deleted were viable but exhibited growth defects. Slow growing mutants expressing Tom40, where residues 321-323 were changed to Ala residues, were isolated but showed TOM complex defects, whereas strains in which residues 321-323 were deleted could not be isolated. Analysis of the assembly of mutant Tom40 precursors in vitro supported a previous model in which Tom40 precursors progress from the 250-kDa intermediate to a 100-kDa form and then assemble into the 400-kDa TOM complex. Surprisingly, when wild type mitochondria containing Tom40 precursors arrested at the 250-kDa intermediate were treated with sodium carbonate, further assembly of intermediates into the TOM complex occurred, suggesting that disruption of protein-protein interactions may facilitate assembly. Import of wild type Tom40 precursor into mitochondria containing a mutant Tom40 lacking residues 40-48 revealed an alternate assembly pathway and demonstrated that the N-terminal region of pre-existing Tom40 molecules in the TOM complex plays a role in the assembly of incoming Tom40 molecules.