Commichau, Fabian M.

[["dc.bibliographiccitation.firstpage","1068"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Molecular BioSystems"],["dc.bibliographiccitation.lastpage","1075"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Pietack, Nico"],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T09:30:00Z"],["dc.date.available","2018-11-07T09:30:00Z"],["dc.date.issued","2013"],["dc.description.abstract","In 2003, an initial study on essential genes in the Gram-positive model bacterium described 271 genes as essential. In the past decade, the functions of many unknown genes and their encoded proteins have been elucidated. Moreover, detailed analyses have revealed that 31 genes that were thought to be essential are in fact non-essential whereas 20 novel essential genes have been described. Thus, 261 genes coding for 259 proteins and two functional RNAs are regarded essential as of January 2013. Among the essential proteins, the largest group is involved in protein synthesis, secretion and protein quality control. Other large sets of essential proteins are involved in lipid biosynthesis, cell wall metabolism and cell division, and DNA replication. Another interesting group of essential proteins protects the cell against endogenous toxic proteins, metabolites, or other intermediates. There are only six essential proteins in B. subtilis, for which no function is known. The functional analysis of these important proteins is predicted to be a key issue in the research on this model organism in the coming years."],["dc.identifier.doi","10.1039/c3mb25595f"],["dc.identifier.isi","000318557100003"],["dc.identifier.pmid","23420519"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10469"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31197"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Royal Soc Chemistry"],["dc.relation.issn","1742-206X"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Essential genes in Bacillus subtilis: a re-evaluation after ten years"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","129"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Molecular Microbiology and Biotechnology"],["dc.bibliographiccitation.lastpage","140"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Pietack, Nico"],["dc.contributor.author","Becher, Doerte"],["dc.contributor.author","Schmidl, Sebastian R."],["dc.contributor.author","Saier, Milton H."],["dc.contributor.author","Hecker, Michael"],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T08:48:00Z"],["dc.date.available","2018-11-07T08:48:00Z"],["dc.date.issued","2010"],["dc.description.abstract","Phosphorylation is an important mechanism of protein modification. In the Gram-positive soil bacterium Bacillus subtilis, about 5% of all proteins are subject to phosphorylation, and a significant portion of these proteins is phosphorylated on serine or threonine residues. We were interested in the regulation of the basic metabolism in B. subtilis. Many enzymes of the central metabolic pathways are phosphorylated in this organism. In an attempt to identify the responsible protein kinase(s), we identified four candidate kinases, among them the previously studied kinase PrkC. We observed that PrkC is indeed able to phosphorylate several metabolic enzymes in vitro. Determination of the phosphorylation sites revealed a remarkable preference of PrkC for threonine residues. Moreover, PrkC often used several phosphorylation sites in one protein. This feature of PrkC-dependent protein phosphorylation resembles the multiple phosphorylations often observed in eukaryotic proteins. The HPr protein of the phosphotransferase system is one of the proteins phosphorylated by PrkC, and PrkC phosphorylates a site (Ser-12) that has recently been found to be phosphorylated in vivo. The agreement between in vivo and in vitro phosphorylation of HPr on Ser-12 suggests that our in vitro observations reflect the events that take place in the cell. Copyright (C) 2010 S. Karger AG, Basel"],["dc.identifier.doi","10.1159/000308512"],["dc.identifier.isi","000278674200001"],["dc.identifier.pmid","20389117"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9309"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21096"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Karger"],["dc.relation.issn","1464-1801"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","In vitro Phosphorylation of Key Metabolic Enzymes from Bacillus subtilis: PrkC Phosphorylates Enzymes from Different Branches of Basic Metabolism"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]