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In 2017, the MeToo hashtag spread across the globe. However, it showed limited success in the Japanese Twittersphere and instead inspired local initiatives such as #WeToo and #Furawādemo ("flower demo"). To understand this reformulation, we analyzed 15 interviews with Japanese social media users and 119 Japanese newspaper articles. The results corroborate the framework we label VTM (values, topics, media), suggesting that an intersection between perceived Japanese values, the topic's gendered and sexual nature, and media affordances explain the movement's local development. While perceived Japanese values clash against those associated with #MeToo, new formulations "soften" the protest by blending in values such as reserve and harmony. Overall, we show how perceptions of popular values rather than values as essential orientations shape activism. Finally, we discuss the study's implications for understanding cultural variance in cyberactivism, highlighting how divergent notions of "safe space" shape such movements.

During the decade of the 1960s a new social science discipline was created. Aaron Wildavsky, along with a small number of other scholars, began focusing their research on public policy studies and the analysis of governmental policy. This article discusses Professor Aaron Wildavsky's original interest in this field, how he institutionalized it by creating a Graduate School of Public Policy at the University of California, Berkeley, and his major contributions to the emerging field. Aaron Wildavsky was one of the preeminent social scientists of the twentieth century, and this article is intended to explain why. Adapted from the source document.

The functional screening of a Pseudacanthotermes militaris termite gut metagenomic library revealed an array of xylan-degrading enzymes, including P. militaris 25 (Pm25), a multimodular glycoside hydrolase family 10 (GH10). Sequence analysis showed details of the unusual domain organization of this enzyme. It consists of one catalytic domain, which is intercalated by two carbohydrate binding modules (CBMs) from family 4. The genes upstream of the genes encoding Pm25 are susC-susD-unk, suggesting Pm25 is a Xyn10C-like enzyme belonging to a polysaccharide utilization locus. The majority of Xyn10C-like enzymes shared the same interrupted domain architecture and were vastly distributed in different xylan utilization loci found in gut Bacteroidetes, indicating the importance of this enzyme in glycan acquisition for gut microbiota. To understand its unusual multimodularity and the possible role of the CBMs, a detailed characterization of the full-length Pm25 and truncated variants was performed. Results revealed that the GH10 catalytic module is specific toward the hydrolysis of xylan. Ligand binding results indicate that the GH10 module and the CBMs act independently, whereas the tandem CBM4s act synergistically with each other and improve enzymatic activity when assayed on insoluble polysaccharides. In addition, we show that the UNK protein upstream of Pm25 is able to bind arabinoxylan. Altogether, these findings contribute to a better understanding of the potential role of Xyn10C-like proteins in xylan utilization systems of gut bacteria. IMPORTANCE Xylan is the major hemicellulosic polysaccharide in cereals and contributes to the recalcitrance of the plant cell wall toward degradation. Members of the Bacteroidetes, one of the main phyla in rumen and human gut microbiota, have been shown to encode polysaccharide utilization loci dedicated to the degradation of xylan. Here, we present the biochemical characterization of a xylanase encoded by a Bacteroidetes strain isolated from the termite gut metagenome. This ...

Intro -- Title Page -- Dedication -- Day 1 -- Day 2 -- Day 3 -- Day 4 -- Day 5 -- Day 6 -- Day 7 -- Day 8 -- Day 9 -- Day 10 -- Day 11 -- Day 12 -- Day 13 -- Day 14 -- Day 15 -- Author's Note -- Acknowledgments -- Helpline Advice -- About the Author -- Copyright.