{"title":"Evaluation of synthetic peptides for direct protein delivery into Saccharomyces cerevisiae.","authors":"Shota Isogai, Ryoya Tanahashi, Hiroshi Takagi, Akira Nishimura","doi":"10.1093/bbb/zbaf111","DOIUrl":"10.1093/bbb/zbaf111","url":null,"abstract":"<p><p>Efficient intracellular delivery of functional proteins into the yeast Saccharomyces cerevisiae remains a major technical challenge due to its rigid cell wall. Here, we report that synthetic peptide tags, particularly penetratin, enable nearly complete delivery of GFP, albeit with substantial cytotoxicity. This method provides a promising non-genetic platform for the intracellular delivery and functional analysis of proteins in yeast systems.</p>","PeriodicalId":9175,"journal":{"name":"Bioscience, Biotechnology, and Biochemistry","volume":" ","pages":"1525-1528"},"PeriodicalIF":1.3,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144673922","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Transcriptional response to elemental sulfur in Geobacter sulfurreducens.","authors":"Masao Inoue, Daiki Fujita, Yukiko Izu, Riku Aono, Hisaaki Mihara","doi":"10.1093/bbb/zbaf106","DOIUrl":"10.1093/bbb/zbaf106","url":null,"abstract":"<p><p>The metal-reducing bacterium Geobacter sulfurreducens PCA is capable of anaerobic respiration using elemental sulfur as an electron acceptor. Despite 3 decades since its isolation, the molecular mechanisms underlying sulfur respiration remain unclear. In this study, we conducted a transcriptome analysis of G. sulfurreducens PCA cultured with and without sublimed sulfur. In the presence of sulfur, 153 genes were significantly up-regulated, while 599 genes were down-regulated. Notably, genes encoding redox proteins involved in energy conservation, particularly multiheme c-type cytochromes, exhibited altered expression patterns. In addition, elemental sulfur induced the transcription of genes associated with sulfur, selenium, and nitrogen metabolism, as well as protein redox homeostasis, DNA repair, and even cell motility. These transcriptional responses may reflect metabolic adaptation to sulfur respiration, redox state alterations, and sulfur-induced stress. Our findings uncover a complex regulatory landscape governing sulfur respiration and provide critical insights into this long-standing biochemical enigma in G. sulfurreducens PCA.</p>","PeriodicalId":9175,"journal":{"name":"Bioscience, Biotechnology, and Biochemistry","volume":" ","pages":"1499-1508"},"PeriodicalIF":1.3,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144688933","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Dehydrogenation of coelenterazine to dehydrocoelenterazine using molecular sieves.","authors":"Mitsuhiro Nakamura, Kazuya Nakayama, Kazuo Matsuda, Satoshi Inouye","doi":"10.1093/bbb/zbaf109","DOIUrl":"10.1093/bbb/zbaf109","url":null,"abstract":"<p><p>Coelenterazine (CTZ) and dehydrocoelenterazine (dCTZ, a dehydrogenated form of CTZ) were first identified in the liver of the luminescent squid Watasenia scintillans. In this report, we demonstrate for the first time that CTZ can be successfully converted to dCTZ using molecular sieves (MS4A/Na+, MS13X/Na+, MS5A/Ca2+, and MS3A/K+) in isopropyl alcohol at 37 °C for 3 h. The conversion efficiency to dCTZ followed the order: MS4A/Na+ = MS13X/Na+ > MS5A/Ca2+ > MS3A/K+. Lower efficiencies observed with modified MS4A (TMS-MS4A, NH4+-MS4A, and H+-MS4A) suggest that cations in the molecular sieves play a crucial role in the dehydrogenation reaction of CTZ. Notably, MS4A recovered from the reaction mixture could be reused without thermal regeneration for dehydration. In purified dCTZ, no residual CTZ was detected using the luciferin-luciferase reaction, and dCTZ can be used as a substrate in luminescence assays to determine enzymatic conversion activity to CTZ.</p>","PeriodicalId":9175,"journal":{"name":"Bioscience, Biotechnology, and Biochemistry","volume":" ","pages":"1425-1431"},"PeriodicalIF":1.3,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144673920","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The aqueous extracts of Inonotus obliquus (Chaga) augment host defense against Listeria monocytogenes infection.","authors":"Akio Nakane, Tatsuji Takahashi, Kenichi Ito, Krisana Asano","doi":"10.1093/bbb/zbaf102","DOIUrl":"10.1093/bbb/zbaf102","url":null,"abstract":"<p><p>Listeria monocytogenes, which grows in host cells intracellularly, is important as an opportunistic pathogen. Extracts of Chaga mushroom, Inonotus obliquus, have been shown to possess various biological activities. This study explores the impact of Chaga extracts on host defense against infection with L. monocytogenes, which induces T-helper (Th)1-type immune response. Chaga extracts enhanced cytokine production including tumor necrosis factor-α, interleukin (IL-6), and IL-12 but suppressed IL-10 production in murine macrophages and dendritic cells. Oral administration of Chaga extracts inhibited the proliferation of L. monocytogenes in the livers of infected mice. Interferon-γ (IFN-γ) and IL-12 production was enhanced in the spleen cell cultures of the extract-treated mice. Chaga extract treatment augmented the clearance of L. monocytogenes from the livers and spleens during re-infection. IFN-γ production was also enhanced in the spleen cell cultures of primarily infected mice. Together, the results indicate that Chaga extracts possess protective potentials for infectious diseases such as listeriosis.</p>","PeriodicalId":9175,"journal":{"name":"Bioscience, Biotechnology, and Biochemistry","volume":" ","pages":"1479-1487"},"PeriodicalIF":1.3,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144636181","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Human cathelicidin peptide LL-37 induces endothelial-to-mesenchymal transition.","authors":"Kaori Suzuki, Mari Ohkuma, Isao Nagaoka","doi":"10.1093/bbb/zbaf112","DOIUrl":"10.1093/bbb/zbaf112","url":null,"abstract":"<p><p>Endothelial-to-mesenchymal transition (EndMT) is a process that causes endothelial cells (ECs) to lose their EC characteristics and transform into mesenchymal cells. Accumulating studies suggest that EndMT is induced in atherosclerotic plaques and contributes to the pathogenesis of atherosclerosis. LL-37 is a multifaceted peptide with antimicrobial and immunomodulatory actions. Interestingly, LL-37 is localized in atherosclerotic plaques, suggesting an association between EndMT and LL-37 in atherosclerosis. Thus, we examined the EndMT-inducing activity of LL-37 using human umbilical vein ECs. LL-37 decreased EC markers but increased mesenchymal cell markers in the cells. LL-37 decreased the vascular network formation of the cells but increased the cell migration, a characteristic function of mesenchymal cells. Finally, the LL-37-induced EndMT was inhibited by Akt and nuclear factor-kappa B (NF-κB) inhibitors, suggesting that LL-37 induces EndMT by activating Akt and NF-κB. These observations speculate a role of LL-37 in the pathogenesis of atherosclerosis as an EndMT inducer.</p>","PeriodicalId":9175,"journal":{"name":"Bioscience, Biotechnology, and Biochemistry","volume":" ","pages":"1464-1473"},"PeriodicalIF":1.3,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144673923","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"A key regulatory region required for the inhibition of proline utilization in the yeast transceptor Can1.","authors":"Ryoya Tanahashi, Hiroshi Takagi, Akira Nishimura","doi":"10.1093/bbb/zbaf110","DOIUrl":"10.1093/bbb/zbaf110","url":null,"abstract":"<p><p>The transceptor Can1 negatively regulates proline utilization in the yeast Saccharomyces cerevisiae. Here, we demonstrated that Can1 physically interacts with the catalytic subunits of protein kinase A (Tpk1, Tpk2, and Tpk3). Furthermore, we identified a specific site in Can1 that is essential for inhibiting proline utilization. These findings provide a mechanistic basis for Can1-mediated metabolic regulation.</p>","PeriodicalId":9175,"journal":{"name":"Bioscience, Biotechnology, and Biochemistry","volume":" ","pages":"1521-1524"},"PeriodicalIF":1.3,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144673919","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Palmitoylation of the fission yeast protein Isp3 is essential for the formation of the outermost layer of the spore wall.","authors":"Takafumi Sakai, Nagisa Minomo, Tomoki Sakaguchi, Yuhei O Tahara, Makoto Miyata, Taro Nakamura","doi":"10.1093/bbb/zbaf104","DOIUrl":"10.1093/bbb/zbaf104","url":null,"abstract":"<p><p>Fission yeast spores possess strong resistance to environmental stresses, largely due to the outermost proteinaceous \"Isp3 layer,\" which comprises Isp3 protein. Isp3 is palmitoylated, and its localization to the spore periphery is impaired in mutants lacking palmitoyltransferase; however, the precise role of Isp3 palmitoylation remains unclear. Here, we found that Isp3-GFP was expressed at wild-type levels in forming spores in mug142∆ cells lacking the palmitoyltransferase catalytic unit; thus, lack of palmitoylation did not reduce Isp3 protein stability. Next, we identified cysteine 7 as the key palmitoylation site essential for Isp3 localization to the spore periphery. Electron microscopy revealed that the Isp3 fibrillar layer was absent in both mug142Δ and isp3-C7S spores. Additionally, the isp3-C7S spores displayed increased sensitivity to alcohol stress, similar to isp3∆ spores. Collectively, these results demonstrate that palmitoylation of Isp3 is essential for the relocation of Isp3 to the spore surface and the assembly of the Isp3 layer.</p>","PeriodicalId":9175,"journal":{"name":"Bioscience, Biotechnology, and Biochemistry","volume":" ","pages":"1444-1455"},"PeriodicalIF":1.3,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144641779","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Podophyllotoxin and α-peltatin inhibit nuclear factor κB activation and gene expression stimulated by a double-stranded RNA analogue in human umbilical vein endothelial cells.","authors":"Yuka Yokota, Piimwara Yarangsee, Kosuke Baba, Saki Sasaki, Hiroyuki Hirano, Hiroyuki Osada, Takao Kataoka","doi":"10.1093/bbb/zbaf108","DOIUrl":"10.1093/bbb/zbaf108","url":null,"abstract":"<p><p>In vascular endothelial cells, proinflammatory cytokines and Toll-like receptor (TLR) ligands up-regulate the expression of adhesion molecules. In the present study, screening of the RIKEN Natural Products Depository chemical libraries identified podophyllotoxin and α-peltatin, which inhibited intercellular adhesion molecule-1 (ICAM-1) expression induced by polyinosinic-polycytidylic acid (Poly(I:C)) as a TLR3 ligand. In human umbilical vein endothelial cells (HUVEC), podophyllotoxin and its derivative α-peltatin inhibited Poly(I:C)-induced increases in the mRNA expression of ICAM-1, vascular cell adhesion molecule-1 (VCAM-1), and E-selectin. In addition, podophyllotoxin and α-peltatin inhibited the Poly(I:C)-induced nuclear translocation of the nuclear factor κB (NF-κB) subunit RelA. Microtubule-targeting agents (colchicine, vinblastine, and paclitaxel) exerted different effects on the Poly(I:C)-induced mRNA expression of ICAM-1, VCAM-1, and E-selectin. Vinblastine potently inhibited nuclear RelA translocation in Poly(I:C)-stimulated HUVEC, whereas colchicine and paclitaxel did not. Collectively, these results demonstrate that podophyllotoxin and α-peltatin inhibited NF-κB activation and mRNA expression by TLR3 stimulation in HUVEC.</p>","PeriodicalId":9175,"journal":{"name":"Bioscience, Biotechnology, and Biochemistry","volume":" ","pages":"1432-1443"},"PeriodicalIF":1.3,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144673924","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Occurrence and characterization of vitamin B12 compounds in traditional Japanese sweet \"kuzu-mochi\" made from fermented wheat starch.","authors":"Fumio Watanabe, Kyohei Koseki, Tomohiro Bito","doi":"10.1093/bbb/zbaf113","DOIUrl":"10.1093/bbb/zbaf113","url":null,"abstract":"<p><p>This study presents the first detailed evidence that commercially available kuzu-mochi products-a traditional Japanese sweet made from fermented wheat starch-are a natural source of vitamin B12 compounds. Microbiological assays and liquid chromatography-tandem mass spectrometry analyses confirmed the presence of vitamin B12 and its analog (pseudovitamin B12) across all tested samples, along with minor corrinoid compounds. Significant variability in vitamin B12 content was noted at approximately 25-152 ng/100 g wet weight, which was probably associated with differences in fermentation-derived microbial communities. Although kuzu-mochi cannot be a primary source of vitamin B12, its role as a supplementary dietary source is remarkable. These findings shed new light on the nutritional potential of traditional fermented foods.</p>","PeriodicalId":9175,"journal":{"name":"Bioscience, Biotechnology, and Biochemistry","volume":" ","pages":"1488-1498"},"PeriodicalIF":1.3,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144706352","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Diversity and ecological roles of alginate lyases in marine and human microbial ecosystems.","authors":"Kohei Ogura","doi":"10.1093/bbb/zbaf105","DOIUrl":"10.1093/bbb/zbaf105","url":null,"abstract":"<p><p>Acidic polysaccharides such as alginate, a key component of brown algae, have unique properties conferred by their carboxyl groups. Alginate is degraded by alginate lyases, a class of polysaccharide lyases (PLs) that cleave uronic acid glycoside bonds via β-elimination. These enzymes, which are classified into various PL families, differ in structure and substrate specificity but frequently share structural motifs including β-helices, β-jelly rolls, and (α/α)6 barrels coupled with antiparallel β-sheets. Moreover, marine bacteria from the genera Alteromonas, Pseudoalteromonas, and Vibrio produce alginate lyases that belong to several PL families that are associated with blue carbon cycling. Furthermore, some Bacteroides species in the human gut have acquired alginate-degrading genes via horizontal transfer from marine bacteria and/or other Bacteroides species. Alginate fermentation by gut microbes can produce short-chain fatty acids with potential prebiotic effects. This review explores alginate lyase diversity, ecological roles, and relevance in both marine and human microbial ecosystems.</p>","PeriodicalId":9175,"journal":{"name":"Bioscience, Biotechnology, and Biochemistry","volume":" ","pages":"1409-1417"},"PeriodicalIF":1.3,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144673921","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}