scholarly journals Photoperiod-dependent regulation of cell growth by PpCCA1a and PpCCA1b genes encoding single-myb clock proteins in the moss Physcomitrella patens

2009 ◽  
Vol 84 (5) ◽  
pp. 379-384 ◽  
Author(s):  
Ryo Okada ◽  
Santosh B. Satbhai ◽  
Setsuyuki Aoki
Keyword(s):  
Cell Growth ◽  
Physcomitrella Patens ◽  
Clock Proteins ◽  
Genes Encoding

scholarly journals Cell-based screen identifies a new potent and highly selective CK2 inhibitor for modulation of circadian rhythms and cancer cell growth

2019 ◽  
Vol 5 (1) ◽  
pp. eaau9060 ◽  
Author(s):  
Tsuyoshi Oshima ◽  
Yoshimi Niwa ◽  
Keiko Kuwata ◽  
Ashutosh Srivastava ◽  
Tomoko Hyoda ◽  
...  
Keyword(s):  
Cell Growth ◽  
Circadian Clock ◽  
Cancer Cell ◽  
Direct Interaction ◽  
Cancer Cell Growth ◽  
X Ray ◽  
Clock Proteins ◽  
Target Deconvolution ◽  
Phenotypic Screen ◽  
Dependent Inhibition

Compounds targeting the circadian clock have been identified as potential treatments for clock-related diseases, including cancer. Our cell-based phenotypic screen revealed uncharacterized clock-modulating compounds. Through affinity-based target deconvolution, we identified GO289, which strongly lengthened circadian period, as a potent and selective inhibitor of CK2. Phosphoproteomics identified multiple phosphorylation sites inhibited by GO289 on clock proteins, including PER2 S693. Furthermore, GO289 exhibited cell type–dependent inhibition of cancer cell growth that correlated with cellular clock function. The x-ray crystal structure of the CK2α-GO289 complex revealed critical interactions between GO289 and CK2-specific residues and no direct interaction of GO289 with the hinge region that is highly conserved among kinases. The discovery of GO289 provides a direct link between the circadian clock and cancer regulation and reveals unique design principles underlying kinase selectivity.

scholarly journals Promoting Cell Growth And Poly-Y-Glutamic Acid Production By Boosting The Synthesis of Alanine And D-Alanyl-D-Alanine In Bacillus Licheniformis

2022 ◽  
Author(s):  
Zheng Zhang ◽  
Penghui He ◽  
Shiying Hu ◽  
Yanqing Yu ◽  
Xiaoting Wang ◽  
...  
Keyword(s):  
Cell Growth ◽  
Microbial Biomass ◽  
Glutamic Acid ◽  
Bacillus Licheniformis ◽  
Alanine Racemase ◽  
High Yield ◽  
Effective Strategy ◽  
Genes Encoding ◽  
Alanine Synthesis ◽  
Glutamic Acid Production

Abstract Objective: The production of some bio-chemicals affected by the cell growth. This study aimed at promoting the cell growth by overexpressing the synthesis of peptidoglycans tetrapeptide tail components to improve poly-γ-glutamic acid (γ-PGA) production. Results: L-alanine, D-alanine and D-alanyl-D-alanine are primary precursors for the synthesis of peptidoglycans. The addition of L-alanine and D-alanine significantly increased both the cell growth and production of γ-PGA. Then, several genes encoding key enzymes for L/D-alanine and D-alanyl-D-alanine biosynthesis were overexpressed respectively, including ald (encoding alanine dehydrogenase), dal (encoding alanine racemase) and ddl (encoding D-alanine ligase). The results showed that the overexpression of genes ald , dal and ddl increased the production of γ-PGA by 19.72%, 15.91% and 60.90%, and increased the microbial biomass by 15.58%, 18.34% and 49.85%, respectively. Moreover, we demonstrated that the overexpression of genes ald , dal and ddl increased γ-PGA production mainly by enhancing cell growth rather than providing more precursors. Conclusions: This work illustrated the importance of the L/D-alanine and D-alanyl-D-alanine synthesis to the cell growth and the high yield of γ-PGA, and provided an effective strategy for producing γ-PGA .

scholarly journals HMGB2 orchestrates the chromatin landscape of senescence-associated secretory phenotype gene loci

2016 ◽  
Vol 215 (3) ◽  
pp. 325-334 ◽  
Author(s):  
Katherine M. Aird ◽  
Osamu Iwasaki ◽  
Andrew V. Kossenkov ◽  
Hideki Tanizawa ◽  
Nail Fatkhutdinov ◽  
...  
Keyword(s):  
Gene Expression ◽  
Cell Growth ◽  
Cellular Senescence ◽  
Growth Arrest ◽  
High Mobility ◽  
Cell Growth Arrest ◽  
Cytokines And Chemokines ◽  
Secreted Factors ◽  
Genes Encoding ◽  
Secretory Phenotype

Cellular senescence is a stable cell growth arrest that is characterized by the silencing of proliferation-promoting genes through compaction of chromosomes into senescence-associated heterochromatin foci (SAHF). Paradoxically, senescence is also accompanied by increased transcription of certain genes encoding for secreted factors such as cytokines and chemokines, known as the senescence-associated secretory phenotype (SASP). How SASP genes are excluded from SAHF-mediated global gene silencing remains unclear. In this study, we report that high mobility group box 2 (HMGB2) orchestrates the chromatin landscape of SASP gene loci. HMGB2 preferentially localizes to SASP gene loci during senescence. Loss of HMGB2 during senescence blunts SASP gene expression by allowing for spreading of repressive heterochromatin into SASP gene loci. This correlates with incorporation of SASP gene loci into SAHF. Our results establish HMGB2 as a novel master regulator that orchestrates SASP through prevention of heterochromatin spreading to allow for exclusion of SASP gene loci from a global heterochromatin environment during senescence.

scholarly journals The Activator of GntII Genes for Gluconate Metabolism, GntH, Exerts Negative Control of GntR-Regulated GntI Genes in Escherichia coli

2003 ◽  
Vol 185 (6) ◽  
pp. 1783-1795 ◽  
Author(s):  
Ryouichi Tsunedomi ◽  
Hanae Izu ◽  
Takuya Kawai ◽  
Kazunobu Matsushita ◽  
Thomas Ferenci ◽  
...  
Keyword(s):  
Gene Expression ◽  
Escherichia Coli ◽  
Cell Growth ◽  
Mutational Analysis ◽  
Carbon Sources ◽  
Negative Control ◽  
Rna Analysis ◽  
Target Sites ◽  
Genes Encoding ◽  
Transcriptional Fusions

ABSTRACT Gluconate is one of the preferred carbon sources of Escherichia coli, and two sets of gnt genes (encoding the GntI and GntII systems) are involved in its transport and metabolism. GntR represses the GntI genes gntKU and gntT, whereas GntH was previously suggested to be an activator for the GntII genes gntV and idnDO-gntWH. The helix-turn-helix residues of the two regulators GntR and GntH exhibit extensive homologies. The similarity between the two regulators prompted analysis of the cross-regulation of the GntI genes by GntH. Repression of gntKU and gntT by GntH, as well as GntR, was indeed observed using transcriptional fusions and RNA analysis. High GntH expression, from cloned gntH or induced through 5-ketogluconate, was required to observe repression of GntI genes. Two GntR-binding elements were identified in the promoter-operator region of gntKU and were also shown to be the target sites of GntH by mutational analysis. However, the GntI genes were not induced by gluconate in the presence of enhanced amounts of GntH, whereas repression by GntR was relieved by gluconate. The repression of GntI genes by GntH is thus unusual in that it is not relieved by the availability of substrate. These results led us to propose that GntH activates GntII and represses the GntI genes in the presence of metabolites derived from gluconate, allowing the organism to switch from the GntI to the GntII system. This cross-regulation may explain the progressive changes in gnt gene expression along with phases of cell growth in the presence of gluconate.

scholarly journals Gene families and evolution of trehalose metabolism in plants

2007 ◽  
Vol 34 (6) ◽  
pp. 550 ◽  
Author(s):  
John E. Lunn
Keyword(s):  
Physcomitrella Patens ◽  
Oryza Sativa L ◽  
Populus Trichocarpa ◽  
Gene Families ◽  
Class I ◽  
Trehalose Metabolism ◽  
Genes Encoding ◽  
Catalytically Active ◽  
Large Families ◽  
Selaginella Moellendorffii

The genomes of Arabidopsis thaliana L., rice (Oryza sativa L.) and poplar (Populus trichocarpa Torr. & A.Gray) contain large families of genes encoding trehalose-phosphate synthase (TPS) and trehalose-phosphatase (TPP). The class I subfamily of TPS genes encodes catalytically active TPS enzymes, and is represented by only one or two genes in most species. A. thaliana is atypical in having four class I TPS genes, three of which (AtTPS2–4) encode unusual short isoforms of TPS that appear to be found only in members of the Brassicaceae family. The class II TPS genes encode TPS-like proteins with a C-terminal TPP-like domain, but there is no experimental evidence that they have any enzymatic activity and their function is unknown. Both classes of TPS gene are represented in the genomes of chlorophyte algae (Ostreococcus species) and non-flowering plants [Physcomitrella patens (Hedw.) Bruch & Schimp.(B.S.G.) and Selaginella moellendorffii (Hieron. in Engl. & Prantl.)]. This survey shows that the gene families encoding the enzymes of trehalose metabolism are very ancient, pre-dating the divergence of the streptophyte and chlorophyte lineages. It also provides a frame of reference for future studies to elucidate the function of trehalose metabolism in plants.

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