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dc.contributor.advisor Stülke, Jörg Prof. Dr.
dc.contributor.author Cascante-Estepa, Nora
dc.date.accessioned 2017-03-29T11:28:16Z
dc.date.available 2017-03-29T11:28:16Z
dc.date.issued 2017-03-29
dc.identifier.uri http://hdl.handle.net/11858/00-1735-0000-0023-3DF6-D
dc.language.iso eng de
dc.rights.uri http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subject.ddc 570 de
dc.title Localization and Function of RNases in Bacillus subtilis de
dc.type doctoralThesis de
dc.contributor.referee Bohnsack, Markus Prof. Dr.
dc.date.examination 2017-02-22
dc.description.abstracteng The ability to adapt to changing environmental conditions is essential for every organism to survive. In bacteria, this adaptation relies on the control of the mRNA synthesis, stability, and turnover, which allows the expression of different sets of proteins as a response to the external conditions. In many bacteria, the enzymes responsible for the degradation of the mRNA interact to form multi-enzyme complexes, the RNA degradosomes. In the Gram-positive model organism Bacillus subtilis, several binary interactions were detected amongst RNA-related proteins in vivo, and it has been hypothesized that an RNA-degrading complex exists in this organism. These interactions involved the endoribonuclease RNase Y, the RNA helicase CshA, the exoribonucleases RNase J1 and PNPase, and the glycolytic enzymes enolase and phosphofructokinase. Moreover, the paralogue of RNase J1, RNase J2 was shown to only interact with RNase J1. However, some of these interactions could not be reproduced and the complex could never be purified as a whole, questioning the possibility of its existence. In this work, I have studied the subcellular localization of the components of the RNA degradosome of B. subtilis. The differential localization of each protein rules out the existence of a stable RNA degradosome. Furthermore, I have studied the interaction and oligomerization between the paralogous RNases J1 and J2 in vivo, and analyzed the importance of the C-terminal domain for this interaction. The results confirm the interaction of the RNases J1 and J2 through the C-terminal domain, and show that they oligomerize as dimers and tetramers. However, it is possible that the tetramers can only be formed in the presence of RNA. Moreover, it seems that the RNase J2 cannot interact with RNA on its own. Although the enzymes of the putative RNA degradosome have been extensively studied, many questions regarding activity and regulation remain open. Amongst them, the enzyme PNPase is one of the best studied, since PNPase from Escherichia coli has been studied for many decades. It has been shown that ATP, c-di-GMP and citrate, amongst others, can regulate its activity. However, the regulation of the PNPase from B. subtilis is not known. In this work, I have studied the effect of citrate, c-di-GMP and c-di-AMP, as well as enolase and phosphofructokinase, on the RNA degradation activity of PNPase. None of these metabolites and enzymes seems to have an effect on this activity. Altogether, these findings contribute to a better understanding of the complex picture of RNA degradation, while opening ways for further investigations. de
dc.contributor.coReferee Feussner, Ivo Prof. Dr.
dc.contributor.thirdReferee Pöggeler, Stefanie Prof. Dr.
dc.contributor.thirdReferee Kramer, Wilfried PD Dr.
dc.contributor.thirdReferee Commichau, Fabian Moritz Dr.
dc.subject.eng Bacillus subtilis, RNA degradosome, RNA processing, RNases, subcellular localization de
dc.identifier.urn urn:nbn:de:gbv:7-11858/00-1735-0000-0023-3DF6-D-8
dc.affiliation.institute Biologische Fakultät für Biologie und Psychologie de
dc.subject.gokfull Biologie (PPN619462639) de
dc.identifier.ppn 883570920

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