In Vitro Flowering of Orange Jessamine (Murraya Paniculata (L.) Jack)

Branch internodes of Murraya pa,icuhtta Ilowcred in vitro on half-strength MT medium containing 5% sucrose supplemented with cytokinins. The cytokinins only induced vcgctative shoots from the epicotyl of seedlings. The highest pcrccntagc of llowcring (76.7% of thc cxplants) was achieved from branch internodes of flowering plants close to the apex, on half-strength MT medium containing 5% sucrose and 0.001 mgl bcnzyladcnine (BA) in light. Flowcring required two days' exposure to BA, but sboot formation could be initiated even without exposure to BA

The WD-repeat protein superfamily in Arabidopsis: conservation and divergence in structure and function

BACKGROUND: The WD motif (also known as the Trp-Asp or WD40 motif) is found in a multitude of eukaryotic proteins involved in a variety of cellular processes. Where studied, repeated WD motifs act as a site for protein-protein interaction, and proteins containing WD repeats (WDRs) are known to serve as platforms for the assembly of protein complexes or mediators of transient interplay among other proteins. In the model plant Arabidopsis thaliana, members of this superfamily are increasingly being recognized as key regulators of plant-specific developmental events. RESULTS: We analyzed the predicted complement of WDR proteins from Arabidopsis, and compared this to those from budding yeast, fruit fly and human to illustrate both conservation and divergence in structure and function. This analysis identified 237 potential Arabidopsis proteins containing four or more recognizable copies of the motif. These were classified into 143 distinct families, 49 of which contained more than one Arabidopsis member. Approximately 113 of these families or individual proteins showed clear homology with WDR proteins from the other eukaryotes analyzed. Where conservation was found, it often extended across all of these organisms, suggesting that many of these proteins are linked to basic cellular mechanisms. The functional characterization of conserved WDR proteins in Arabidopsis reveals that these proteins help adapt basic mechanisms for plant-specific processes. CONCLUSIONS: Our results show that most Arabidopsis WDR proteins are strongly conserved across eukaryotes, including those that have been found to play key roles in plant-specific processes, with diversity in function conferred at least in part by divergence in upstream signaling pathways, downstream regulatory targets and /or structure outside of the WDR regions

Online Assessment During Covid-19 Pandemic: EFL Teachers' Perspectives and Their Practices

The Covid-19 pandemic made a change in learning activities from face-to-face into online distance learning. Meanwhile, teachers need to evaluate student achievements weekly even during the Covid-19 pandemic. This study aims to find out about teachers' perspectives and their practices on the use of online assessment during Covid-19 in the context of ELT classroom. A case study design was used to answer the purpose of this research. An open-ended questionnaire and online interviews were performed to collect the data. This study revealed the teachers had a negative perception about online assessment during the Covid-19 pandemic. They got some obstacles while conducting the assessment test such as (1) the internet connection; (2) the validity of the assessment; (3) and the low of students' enthusiasm. However, in practice, during Covid-19, the use of online assessment helps the teachers in distributing the material and assessing students' achievement. Implications for perception and practice are also discussed

Crystal structure of peroxisomal targeting signal-2 bound to its receptor complex Pex7p–Pex21p

ペルオキシソーム病RCDP-1の分子機構の解明.京都大学プレスリリース.2013-07-01.Appropriate targeting of matrix proteins to peroxisomes is mainly directed by two types of peroxisomal targeting signals, PTS1 and PTS2. Although the basis of PTS1 recognition has been revealed by structural studies, that of PTS2 recognition remains elusive. Here we present the crystal structure of a heterotrimeric PTS2-recognition complex from Saccharomyces cerevisiae, containing Pex7p, the C-terminal region of Pex21p and the PTS2 of the peroxisomal 3-ketoacyl-CoA thiolase. Pex7p forms a β-propeller structure and provides a platform for cooperative interactions with both the amphipathic PTS2 helix and Pex21p. The C-terminal region of Pex21p directly covers the hydrophobic surfaces of both Pex7p and PTS2, and the resulting hydrophobic core is the primary determinant of stable complex formation. Together with in vivo and in vitro functional assays of Pex7p and Pex21p variants, our findings reveal the molecular mechanism of PTS2 recognition