Teacher Attitudes and Perceptions Toward Students with Mild Disabilities

Students with mild disabilities are spending the majority of their school day in general education classrooms. However, their academic engagement and outcomes are not always favorable and teachers are often unprepared to present curricula in a way that is engaging and accessible for students at every skill level. A Theory of Academic Engagement was developed that addressed a process for increasing engagement and outcomes for students with mild disabilities. A survey was developed and distributed to practicing elementary level teachers in five western states to investigate teachers’ knowledge of Universal Design for Learning (UDL) as well as their attitudes and perceptions toward students with mild disabilities in their classrooms. Both the UDL survey items and the Attitudes and Perceptions items were divided into subfactors and each subfactor was used to address the research questions. In addition to a rating scale, the survey included 4 open-ended written response questions. The findings revealed that while most teachers had some understanding of UDL, they did not have the depth of knowledge or training to implement it effectively. Further, while teachers’ attitudes and perceptions of students with mild disabilities were positive, they expressed frustration with a lack of support and proper training. In addition, a discussion of the results as well as implications and directions for future research are included

Lactose Transport System of Streptococcus thermophilus. The Role of Histidine Residues

The lactose transport protein (LacS) of Streptococcus thermophilus is a chimeric protein consisting of an amino-terminal carrier domain and a carboxyl-terminal phosphoenolpyruvate:sugar phosphotransferase system (PTS) IIA protein domain. The histidine residues of LacS were changed individually into glutamine or arginine residues. Of the 11 histidine residues present in LacS, only the His-376 substitution in the carrier domain significantly affected sugar transport. The region around His-376 was found to exhibit sequence similarity to the region around His-322 of the lactose transport protein (LacY) of Escherichia coli, which has been implicated in sugar binding and in coupling of sugar and H+ transport. The H376Q mutation resulted in a reduced rate of uptake and altered affinity for lactose (beta-galactoside), melibiose (alpha-galactoside), and the lactose analog methyl-beta-D-thiogalactopyranoside. Similarly, the extent of accumulation of the galactosides by cells expressing LacS(H376Q) was highly reduced in comparison to cells bearing the wild-type protein. Nonequilibrium exchange of lactose and methyl-beta-D-thiogalactopyranoside by the H376Q mutant was approximately 2-fold reduced in comparison to the activity of the wild-type transport protein. The data indicate that His-376 is involved in sugar recognition and is important, but not essential, for the cotransport of protons and galactosides. The carboxyl-terminal domain of LacS contains 2 histidine residues (His-537 and His-552) that are conserved in seven homologous IIA protein(s) (domains) of PTSs. P-enolpyruvate-dependent phosphorylation of wild-type LacS, but not of the mutant H552Q, was demonstrated using purified Enzyme I and HPr, the general energy coupling proteins of the PTS, and inside-out membrane vesicles isolated from E. coli in which the lactose transport gene was expressed. The His-537 and His-552 mutations did not affect transport activity when the corresponding genes were expressed in E. coli