Stülke, Jörg

[["dc.bibliographiccitation.artnumber","1328"],["dc.bibliographiccitation.journal","Frontiers in microbiology"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Blötz, Cedric"],["dc.contributor.author","Treffon, Katrin"],["dc.contributor.author","Kaever, Volkhard"],["dc.contributor.author","Schwede, Frank"],["dc.contributor.author","Hammer, Elke"],["dc.contributor.author","Stülke, Jörg"],["dc.date.accessioned","2019-07-09T11:43:38Z"],["dc.date.available","2019-07-09T11:43:38Z"],["dc.date.issued","2017"],["dc.description.abstract","Bacteria often use cyclic dinucleotides as second messengers for signal transduction. While the classical molecule c-di-GMP is involved in lifestyle selection, the functions of the more recently discovered signaling nucleotide cyclic di-AMP are less defined. For many Gram-positive bacteria, c-di-AMP is essential for growth suggesting its involvement in a key cellular function. We have analyzed c-di-AMP signaling in the genome-reduced pathogenic bacterium Mycoplasma pneumoniae. Our results demonstrate that these bacteria produce c-di-AMP, and we could identify the diadenylate cyclase CdaM (MPN244). This enzyme is the founding member of a novel family of diadenylate cyclases. Of two potential c-di-AMP degrading phosphodiesterases, only PdeM (MPN549) is active in c-di-AMP degradation, whereas NrnA (MPN140) was reported to degrade short oligoribonucleotides. As observed in other bacteria, both the c-di-AMP synthesizing and the degrading enzymes are essential for M. pneumoniae suggesting control of a major homeostatic process. To obtain more insights into the nature of this process, we have identified a c-di-AMP-binding protein from M. pneumoniae, KtrC. KtrC is the cytoplasmic regulatory subunit of the low affinity potassium transporter KtrCD. It is established that binding of c-di-AMP inhibits the KtrCD activity resulting in a limitation of potassium uptake. Our results suggest that the control of potassium homeostasis is the essential function of c-di-AMP in M. pneumoniae."],["dc.identifier.doi","10.3389/fmicb.2017.01328"],["dc.identifier.pmid","28751888"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14609"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58934"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1664-302X"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","570"],["dc.title","Identification of the Components Involved in Cyclic Di-AMP Signaling in Mycoplasma pneumoniae"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2853"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","NUCLEIC ACIDS RESEARCH"],["dc.bibliographiccitation.lastpage","2864"],["dc.bibliographiccitation.volume","32"],["dc.contributor.author","Schilling, Oliver"],["dc.contributor.author","Langbein, Ines"],["dc.contributor.author","Müller, Michael"],["dc.contributor.author","Schmalisch, Matthias H."],["dc.contributor.author","Stülke, Jörg"],["dc.date.accessioned","2019-07-10T08:12:53Z"],["dc.date.available","2019-07-10T08:12:53Z"],["dc.date.issued","2004"],["dc.description.abstract","The Gram-positive soil bacterium Bacillus subtilis transports glucose by the phosphotransferase system. The genes for this system are encoded in the ptsGHI operon. The expression of this operon is controlled at the level of transcript elongation by a protein-dependent riboswitch. In the absence of glucose a transcriptional terminator prevents elongation into the structural genes. In the presence of glucose, the GlcT protein is activated and binds and stabilizes an alternative RNA structure that overlaps the terminator and prevents termination. In this work, we have studied the structural and sequence requirements for the two mutually exclusive RNA structures, the terminator and the RNA antiterminator (the RAT sequence). In both cases, the structure seems to be more important than the actual sequence. The number of paired and unpaired bases in the RAT sequence is essential for recognition by the antiterminator protein GlcT. In contrast, mutations of individual bases are well tolerated as long as the general structure of the RAT is not impaired. The introduction of one additional base in the RAT changed its structure and resulted in complete loss of interaction with GlcT. In contrast, this mutant RAT was efficiently recognized by a different B.subtilis antitermination protein, LicT."],["dc.identifier.fs","28429"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/4114"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61066"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","0305-1048"],["dc.relation.issn","1362-4962"],["dc.relation.orgunit","Fakultät für Biologie und Psychologie"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","570"],["dc.title","A protein-dependent riboswitch controlling ptsGHI operon expression in Bacillus subtilis: RNA structure rather than sequence provides interaction specificity."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","99"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","ACS Synthetic Biology"],["dc.bibliographiccitation.lastpage","08"],["dc.contributor.author","Aguilar Suarez, Rocio"],["dc.contributor.author","Stülke, Jörg"],["dc.contributor.author","van Dijl, Jan Maarten"],["dc.date.accessioned","2019-07-09T11:50:24Z"],["dc.date.available","2019-07-09T11:50:24Z"],["dc.date.issued","2018"],["dc.description.abstract","The availability of complete genome sequences and the definition of essential gene sets were fundamental in the start of the genome engineering era. In a recent study, redundant and unnecessary genes were systematically deleted from the Gram-positive bacterium Bacillus subtilis, an industrial production host of high-value secreted proteins. This culminated in strain PG10, which lacks about 36% of the genome, thus representing the most minimal Bacillus chassis currently available. Here, we show that this 'miniBacillus' strain has synthetic traits that are favorable for producing 'difficult-to-produce proteins'. As exemplified with different staphylococcal antigens, PG10 overcomes several bottlenecks in protein production related to the secretion process and instability of the secreted product. These findings show for the first time that massive genome reduction can substantially improve secretory protein production by a bacterial expression host, and underpin the high potential of genome-engineered strains as future cell factories."],["dc.identifier.doi","10.1021/acssynbio.8b00342"],["dc.identifier.pmid","30540431"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15933"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59767"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","info:eu-repo/grantAgreement/EC/H2020/720776/EU//Rafts4Biotech"],["dc.relation.issn","2161-5063"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.subject.ddc","570"],["dc.title","Less is more: towards a genome-reduced Bacillus cell factory for 'difficult proteins'"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]