40 research outputs found

    Examining the Cultural Validity of Fear Survey Schedule for Children: The Contemporary Fears of Turkish Children and Adolescents

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    The authors examined the cultural validity of Fear Survey Schedule for Children (FSSC-AM) developed by J. J. Burnham (2005) with Turkish children. The relationships between demographic variables and the level of fear were also tested. Three independent data sets were used. The first data set comprised 676 participants (321 women and 355 men) and was used for examining factor structure and internal reliability of FSSC. The second data set comprised 639 participants (321 women and 318 men) and was used for testing internal reliability and to confirm the factor structure of FSCC. The third data set comprised 355 participants (173 women and 182 men) and used for analyses of test-retest reliability, inter-item reliability, and convergent validity for the scores of FSSC. The sum of the first and second samples (1,315 participants; 642 women and 673 men) was used for testing the relationships between demographic variables and the level of fear. Results indicated that FSSC is a valid and reliable instrument to examine Turkish children's and adolescents' fears between the ages of 8 and 18years. The younger, female, children of low-income parents reported a higher level of fear. The findings are discussed in light of the existing literature

    Role of Arc1p in the modulation of yeast glutamyl-tRNA synthetase activity

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    Yeast methionyl-tRNA synthetase (MetRS) and glutamyl-tRNA synthetase (GluRS) possess N-terminal extensions that bind the cofactor Arc1p in trans. The strength of GluRS-Arc1p interaction is high enough to allow copurification of the two macromolecules in a 1:1 ratio, in contrast to MetRS. Deletion analysis from the C-terminal end of the GluRS appendix combined with previous N-terminal deletions of GluRS allows restriction of the Arc1p binding site to the 110-170 amino acid region of GluRS. This region has been shown to correspond to a novel protein-protein interaction domain present in both GluRS and Arc1p but not in MetRS [Galani, K., Grosshans, H., Deinert, K., Hurt, E. C., and Simos, G. (2001) EMBO J. 20, 6889-6898]. The GluRS apoenzyme fails to show significant kinetics of tRNA aminoacylation and charges unfractionated yeast tRNA at a level 10-fold reduced compared to Arc1p-bound GluRS. The Km values for tRNA Glu measured in the ATP-PPi exchange were similar for the two forms of GluRS, whereas kcat is increased 2-fold in the presence of Arc1p. Band-shift analysis revealed a 100-fold increase in tRNA binding affinity when Arc1p is bound to GluRS. This increase requires the RNA binding properties of the full-length Arc1p since Arc1p N domain leaves the K d of GluRS for tRNA unchanged. Transcripts of yeast tRNA Glu were poor substrates for measuring tRNA aminoacylation and could not be used to clarify whether Arc1p has a specific effect on the tRNA charging reaction

    Differential Effects of Replacing Escherichia coli Ribosomal Protein L27 with Its Homologue from Aquifex aeolicus

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    The rpmA gene, which encodes 50S ribosomal subunit protein L27, was cloned from the extreme thermophile Aquifex aeolicus, and the protein was overexpressed and purified. Comparison of the A. aeolicus protein with its homologue from Escherichia coli by circular dichroism analysis and proton nuclear magnetic resonance spectroscopy showed that it readily adopts some structure in solution that is very stable, whereas the E. coli protein is unstructured under the same conditions. A mutant of E. coli that lacks L27 was found earlier to be impaired in the assembly and function of the 50S subunit; both defects could be corrected by expression of E. coli L27 from an extrachromosomal copy of the rpmA gene. When A. aeolicus L27 was expressed in the same mutant, an increase in the growth rate occurred and the “foreign” L27 protein was incorporated into E. coli ribosomes. However, the presence of A. aeolicus L27 did not promote 50S subunit assembly. Thus, while the A. aeolicus protein can apparently replace its E. coli homologue functionally in completed ribosomes, it does not assist in the assembly of E. coli ribosomes that otherwise lack L27. Possible explanations for this paradoxical behavior are discussed
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