PUMA publications for /tag/sequenceWed Mar 05 15:52:38 CET 2025Nature Communicationsaug13315Decoding a cancer-relevant splicing decision in the {RON} proto-oncogene using high-throughput mutagenesis92018Acid, Alternative Analysis, Base Binding Cells, Exons, F-H, Group HEK293 Heterogeneous-Nuclear Humans, Introns, Kinases, Linear MCF-7 Mas, Models, Mutagenesis, Mutation, Neoplasms, Nucleic Protein-Tyrosine Proteins, Proto-Oncogene RNA RNA-Binding Receptor Regulatory Ribonucleoprotein Sequence Sequence, Sequences, Sites, Splicing, Mutations causing aberrant splicing are frequently implicated in human diseases including cancer. Here, we establish a high-throughput screen of randomly mutated minigenes to decode the cis-regulatory landscape that determines alternative splicing of exon 11 in the proto-oncogene MST1R (RON). Mathematical modelling of splicing kinetics enables us to identify more than 1000 mutations affecting RON exon 11 skipping, which corresponds to the pathological isoform RON∆165. Importantly, the effects correlate with RON alternative splicing in cancer patients bearing the same mutations. Moreover, we highlight heterogeneous nuclear ribonucleoprotein H (HNRNPH) as a key regulator of RON splicing in healthy tissues and cancer. Using iCLIP and synergy analysis, we pinpoint the functionally most relevant HNRNPH binding sites and demonstrate how cooperative HNRNPH binding facilitates a splicing switch of RON exon 11. Our results thereby offer insights into splicing regulation and the impact of mutations on alternative splicing in cancer.Tue Jun 23 15:14:59 CEST 2020Determining Power Transformers’ Sequence of Maintenance and Repair in Power Grids2010Determining Grids Maintenance Power Repair Sequence Transformers’ in Mon Jun 15 14:37:54 CEST 2020IEEE Transactions on Dielectrics and Electrical InsulationOctober51789-1797Determining Power Transformers' Sequence of Service in Power Grids182011Determining Grids Power Sequence Service Transformers of Tue Apr 03 14:38:03 CEST 2018Angewandte Chemie International Editionaug326106Extending the {(Mo)Mo5}12M30 Capsule Keplerate Sequence: A {Cr30} Cluster of S=3/2 Metal Centers with a {Na(H2O)12} Encapsulate462007Keplerate capsule sequence Mon Feb 19 14:58:22 CET 2018Acoustics, Speech and Signal Processing (ICASSP), 2016 IEEE International Conference on5315--5319Sequence summarizing neural network for speaker adaptation2016adaptation, i-vector, sequence speaker summarizing Fri Feb 09 13:18:17 CET 2018Appl. Environ. Microbiol.jan2419--427Acetohydroxyacid synthase, a novel target for improvement of {L}-lysine production by {Corynebacterium} glutamicum752009Acetolactate Acid, Bacterial Butyrates Corynebacterium Deletion, Enzyme Expression Gene Inhibitors, Isoleucine, Kinetics, Leucine, Lysine, Profiling, Proteins, Pyruvic Sequence Synthase, Valine, glutamicum, myown The influence of acetohydroxy acid synthase (AHAS) on L-lysine production by Corynebacterium glutamicum was investigated. An AHAS with a deleted C-terminal domain in the regulatory subunit IlvN was engineered by truncating the ilvN gene. Compared to the wild-type AHAS, the newly constructed enzyme showed altered kinetic properties, i.e., (i) an about twofold-lower K(m) for the substrate pyruvate and an about fourfold-lower V(max); (ii) a slightly increased K(m) for the substrate alpha-ketobutyrate with an about twofold-lower V(max); and (iii) insensitivity against the inhibitors L-valine, L-isoleucine, and L-leucine (10 mM each). Introduction of the modified AHAS into the L-lysine producers C. glutamicum DM1729 and DM1933 increased L-lysine formation by 43\% (30 mM versus 21 mM) and 36\% (51 mM versus 37 mM), respectively, suggesting that decreased AHAS activity is linked to increased L-lysine formation. Complete inactivation of the AHAS in C. glutamicum DM1729 and DM1933 by deletion of the ilvB gene, encoding the catalytic subunit of AHAS, led to L-valine, L-isoleucine, and L-leucine auxotrophy and to further-improved L-lysine production. In batch fermentations, C. glutamicum DM1729 Delta ilvB produced about 85\% more L-lysine (70 mM versus 38 mM) and showed an 85\%-higher substrate-specific product yield (0.180 versus 0.098 mol C/mol C) than C. glutamicum DM1729. Comparative transcriptome analysis of C. glutamicum DM1729 and C. glutamicum DM1729 Delta ilvB indicated transcriptional differences for about 50 genes, although not for those encoding enzymes involved in the L-lysine biosynthetic pathway.Fri Feb 09 13:18:17 CET 2018J. Mol. Microbiol. Biotechnol.3-4236--239{RamB} is an activator of the pyruvate dehydrogenase complex subunit {E}1p gene in {Corynebacterium} glutamicum162009(Lipoamide) Acetates, Bacterial Bacterial, Base Corynebacterium Data, Dehydrogenase Expression Gene Molecular Proteins, Pyruvate Regulation, Sequence Sequence, glutamicum, myown In Corynebacterium glutamicum, the transcriptional regulator RamB negatively controls the expression of genes involved in acetate metabolism. Here we show that during growth in media containing glucose and in complex medium without glucose RamB activates expression of the aceE gene, encoding the E1p subunit of the pyruvate dehydrogenase complex. Thus, RamB functions both as repressor and as activator in C. glutamicum.sequenceCommunity for tag(s) sequence