Hubungan Pengetahuan Agama Islam terhadap Pemahaman Nilai-Nilai Pancasila Siswa di SMP Royal Wells Middle Schools

The religious, cultural, and ethnic diversity of Indonesia is well-known. Differences in understanding, nationality, and religion are frequently the primary causes of existing difficulties, to name just a few. This study sought to ascertain the relationship between eighth-grade students at SMP Royal Wells Middle School's knowledge and understanding of Islam and the Pancasila ideals. This study used a quantitative research method using a correlational approach. Understanding of Pancasila values is variable Y in this study, while Islamic religious knowledge is variable X. The population of this study consisted of 20 students, and the method of data collection used in it was distributing a questionnaire to eighth-graders at Royal Wells Middle School. The findings revealed a moderate link between Pancasila ideals and knowledge and understanding of Islam. Students can thus use the information on religious values and Pancasila both in the context of the classroom and in the community.

A novel <it>Geobacteraceae</it>-specific outer membrane protein J (OmpJ) is essential for electron transport to Fe (III) and Mn (IV) oxides in <it>Geobacter sulfurreducens</it>

<p>Abstract</p> <p>Background</p> <p>Metal reduction is thought to take place at or near the bacterial outer membrane and, thus, outer membrane proteins in the model dissimilatory metal-reducing organism <it>Geobacter sulfurreducens </it>are of interest to understand the mechanisms of Fe(III) reduction in the <it>Geobacter </it>species that are the predominant Fe(III) reducers in many environments. Previous studies have implicated periplasmic and outer membrane cytochromes in electron transfer to metals. Here we show that the most abundant outer membrane protein of <it>G. sulfurreducens</it>, OmpJ, is not a cytochrome yet it is required for metal respiration.</p> <p>Results</p> <p>When outer membrane proteins of <it>G. sulfurreducens </it>were separated via SDS-PAGE, one protein, designated OmpJ (outer membrane protein J), was particularly abundant. The encoding gene, which was identified from mass spectrometry analysis of peptide fragments, is present in other <it>Geobacteraceae</it>, but not in organisms outside this family. The predicted localization and structure of the OmpJ protein suggested that it was a porin. Deletion of the <it>ompJ </it>gene in <it>G. sulfurreducens </it>produced a strain that grew as well as the wild-type strain with fumarate as the electron acceptor but could not grow with metals, such as soluble or insoluble Fe (III) and insoluble Mn (IV) oxide, as the electron acceptor. The heme <it>c </it>content in the mutant strain was ca. 50% of the wild-type and there was a widespread loss of multiple cytochromes from soluble and membrane fractions. Transmission electron microscopy analyses of mutant cells revealed an unusually enlarged periplasm, which is likely to trigger extracytoplasmic stress response mechanisms leading to the degradation of periplasmic and/or outer membrane proteins, such as cytochromes, required for metal reduction. Thus, the loss of the capacity for extracellular electron transport in the mutant could be due to the missing <it>c</it>-type cytochromes, or some more direct, but as yet unknown, role of OmpJ in metal reduction.</p> <p>Conclusion</p> <p>OmpJ is a putative porin found in the outer membrane of the model metal reducer <it>G. sulfurreducens </it>that is required for respiration of extracellular electron acceptors such as soluble and insoluble metals. The effect of OmpJ in extracellular electron transfer is indirect, as OmpJ is required to keep the integrity of the periplasmic space necessary for proper folding and functioning of periplasmic and outer membrane electron transport components. The exclusive presence of <it>ompJ </it>in members of the <it>Geobacteraceae </it>family as well as its role in metal reduction suggest that the <it>ompJ </it>sequence may be useful in tracking the growth or activity of <it>Geobacteraceae </it>in sedimentary environments.</p

Aberrant expression of miR-141 and nuclear receptor small heterodimer partner in clinical samples of prostate cancer.

BACKGROUND: Prostate cancer (PCa) is the second most common cancer in men worldwide. Currently, prostate-specific antigen (PSA) test and digital rectal exam are the main screening tests used for PCa diagnosis. However, due to the low specificity of these tests, new alternative biomarkers such as deregulated RNAs and microRNAs have been implemented. OBJECTIVES: Aberrant expression of small heterodimer partner gene (SHP, NR0B2) and mir-141 are reported in various cancers. The aim of this study was to investigate the SHP and miR-141 expression level in tissue samples of prostate cancer. METHODS: The expression level of SHP gene and miR-141 was assessed by real time PCR and their relative amounts were calculated by the Δ⁢ΔCT method. Also, IHC technique was used to determine the expression level of SHP protein. RESULTS: The miR-141 was significantly up-regulated in the samples of metastatic tumors compared to localized tumor samples (P< 0.001, 31.17-fold change). Tumor samples showed lower SHP mRNA expression level than BPH samples (p= 0.014, 4.7-fold change). The results of paired t-test analysis showed there was no significant difference between the SHP gene expression in PCa samples and their matched tumor-adjacent normal tissue (p= 0.5). CONCLUSIONS: The data obtained in our study confirm the involvement of miR-141 in PCa progression and metastasis. These effects could be mediated by AR via down-regulation of its co-repressor protein, i.e., SHP. KEYWORDS: Immunohistochemistry; Prostate cancer; SHP gene; biomarker; gene expression; miR-141; nuclear receptor

The Mosaic Genome of Anaeromyxobacter dehalogenans Strain 2CP-C Suggests an Aerobic Common Ancestor to the Delta-Proteobacteria

©2008 Thomas et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.doi:10.1371/journal.pone.0002103Anaeromyxobacter dehalogenans strain 2CP-C is a versaphilic delta-Proteobacterium distributed throughout many diverse soil and sediment environments. 16S rRNA gene phylogenetic analysis groups A. dehalogenans together with the myxobacteria, which have distinguishing characteristics including strictly aerobic metabolism, sporulation, fruiting body formation, and surface motility. Analysis of the 5.01 Mb strain 2CP-C genome substantiated that this organism is a myxobacterium but shares genotypic traits with the anaerobic majority of the delta-Proteobacteria (i.e., the Desulfuromonadales). Reflective of its respiratory versatility, strain 2CP-C possesses 68 genes coding for putative c-type cytochromes, including one gene with 40 heme binding motifs. Consistent with its relatedness to the myxobacteria, surface motility was observed in strain 2CP-C and multiple types of motility genes are present, including 28 genes for gliding, adventurous (A-) motility and 17 genes for type IV pilus-based motility (i.e., social (S-) motility) that all have homologs in Myxococcus xanthus. Although A. dehalogenans shares many metabolic traits with the anaerobic majority of the delta- Proteobacteria, strain 2CP-C grows under microaerophilic conditions and possesses detoxification systems for reactive oxygen species. Accordingly, two gene clusters coding for NADH dehydrogenase subunits and two cytochrome oxidase gene clusters in strain 2CP-C are similar to those in M. xanthus. Remarkably, strain 2CP-C possesses a third NADH dehydrogenase gene cluster and a cytochrome cbb3 oxidase gene cluster, apparently acquired through ancient horizontal gene transfer from a strictly anaerobic green sulfur bacterium. The mosaic nature of the A. dehalogenans strain 2CP-C genome suggests that the metabolically versatile, anaerobic members of the delta-Proteobacteria may have descended from aerobic ancestors with complex lifestyles