dc.contributor.advisor | Stülke, Jörg Prof. Dr. | de |
dc.contributor.author | Rothe, Fabian | de |
dc.date.accessioned | 2013-01-14T15:06:51Z | de |
dc.date.available | 2013-01-30T23:51:03Z | de |
dc.date.issued | 2012-11-12 | de |
dc.identifier.uri | http://hdl.handle.net/11858/00-1735-0000-000D-EF83-8 | de |
dc.identifier.uri | http://dx.doi.org/10.53846/goediss-1457 | |
dc.description.abstract | Die Regulation der Genexpression ist
essentiell für alle Bakterien und ermöglicht die Anpassung an sich
verändernde Lebensbedingungen. Verschiedene Transkriptions- und
Translationsfaktoren haben bei dieser Regulation eine große
Bedeutung. Die Antiterminationsproteine der BglG/ SacY-Familie sind
in Bakterien weit verbreitet und steuern die Expression von Genen
und Operons, die an der Aufnahme und Verwertung von
Kohlenstoffquellen beteiligt sind. Die substrat- und
phosphorylierungsabhängige Aktivierung der Proteine der BglG/
SacY-Familie erlaubt es ihnen, an ihre Ziel-RNA zu binden und
ermöglicht das Fortschreiten der blockierten Transkription. Der
Transkriptionsfaktor BglG aus Escherichia coli ist | de |
dc.format.mimetype | application/pdf | de |
dc.language.iso | ger | de |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/ | de |
dc.title | Regulation der Aktivität und Lokalisation von Antiterminatorproteinen der BglG-Familie | de |
dc.type | doctoralThesis | de |
dc.title.translated | Regulation of the Activity and Localization of BglG family Antiterminator Proteins | de |
dc.contributor.referee | Stülke, Jörg Prof. Dr. | de |
dc.date.examination | 2012-03-23 | de |
dc.subject.dnb | 570 Biowissenschaften, Biologie | de |
dc.subject.gok | WUE 200 | de |
dc.subject.gok | WUK 000 | de |
dc.subject.gok | WJL 200 | de |
dc.description.abstracteng | The regulation of gene expression is
essential for all bacteria and allows adapting to changing life
conditions. Different transcription and translation factors have an
important impact on gene regulation. The antermination proteins of
the BglG/ SacY family are widely spread. They control the
expression of genes and operons which are involved in the uptake
and utilization of different carbon sources. The substrate and
phosphorylation dependent activation of the BglG/ SacY family
proteins enable these antiterminators to bind their target RNA and
allow proceeding the blocked transcription. The transcription
factor BglG of Escherichia coli is equivalent to LicT of
Bacillus subtilis. Nobody has yet found out whether these
two antitermination proteinsare identical and if they have the same
function in both organisms. In contrast to LicT, the activation
mechanism of BglG is not fully answered yet. Compared to BglG the
localization of active and inactive LicT is also unclear. In this
work it was shown that BglG is phosphorylated and activated by HPr
or FruB which is a homolog to HPr. Furthermore, the phosphorylation
dependent dynamic localization of LicT was detected. In vitro
experiments could show that BglG is phosphorylated by HPr (or FruB)
and thereby activated at histidine-208. Moreover, fluorescence
microscopy detected, that inactive LicT (in the absence of
beta-glucosides) is constantly distributed in the cytoplasm and
accumulates in the cell poles in its active state (after the
addition of beta-glucosides). Mutation analysis of the conserved
phosphorylation sites of LicT revealed that the state of
phosphorylation has an influence on the dynamic localization of
LicT regardless of the LicT activity. The results show that the
control mechanism of E. coli BglG is identical to B.
subtilis LicT and to the other members of BglG / SacY family.
Moreover, it was found that the LicT controlled regulation of gene
expression is more than a simple mechanism, but rather a highly
dynamic process. These observations suggest that there must be more
dynamic localization processes among the many regulatory
mechanisms. Further studies may elucidate those factors which
influence post-translational modifications and the dynamic protein
localization. | de |
dc.contributor.coReferee | Tittmann, Kai Prof. Dr. | de |
dc.contributor.thirdReferee | Seiler, Stephan PD Dr. | de |
dc.subject.topic | Biology (incl. Psychology) | de |
dc.subject.ger | LicT | de |
dc.subject.ger | BglG | de |
dc.subject.ger | Phosphorylierung | de |
dc.subject.ger | Antitermination | de |
dc.subject.ger | RNA-Regulation | de |
dc.subject.ger | Escherichia coli | de |
dc.subject.ger | Bacillus subtilis | de |
dc.subject.ger | dynamische Proteinlokalisation | de |
dc.subject.ger | Phosphotransferasesystem | de |
dc.subject.ger | Genregulation | de |
dc.subject.ger | FruB | de |
dc.subject.ger | HPr | de |
dc.subject.eng | LicT | de |
dc.subject.eng | BglG | de |
dc.subject.eng | phosphorylation | de |
dc.subject.eng | antiterminator | de |
dc.subject.eng | RNA regulation | de |
dc.subject.eng | Escherichia coli | de |
dc.subject.eng | Bacillus subtilis | de |
dc.subject.eng | dynamic protein localisation | de |
dc.subject.eng | phosphotransferase system | de |
dc.subject.eng | gene regulation | de |
dc.subject.eng | FruB | de |
dc.subject.eng | HPr | de |
dc.subject.bk | 42.30 | de |
dc.subject.bk | 42.13 | de |
dc.identifier.urn | urn:nbn:de:gbv:7-webdoc-3789-6 | de |
dc.identifier.purl | webdoc-3789 | de |
dc.affiliation.institute | Biologische Fakultät | de |
dc.identifier.ppn | 73131235X | de |