Heininger, Annika U.

[["dc.bibliographiccitation.firstpage","320"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","RNA Biology"],["dc.bibliographiccitation.lastpage","330"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Heininger, Annika U."],["dc.contributor.author","Hackert, Phillip"],["dc.contributor.author","Andreou, Alexandra Z."],["dc.contributor.author","Boon, Kum-Loong"],["dc.contributor.author","Memet, Indira"],["dc.contributor.author","Prior, Mira"],["dc.contributor.author","Clancy, Anne"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Schleiff, Enrico"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Enderlein, Jörg"],["dc.contributor.author","Klostermeier, Dagmar"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2017-09-07T11:54:35Z"],["dc.date.available","2017-09-07T11:54:35Z"],["dc.date.issued","2016"],["dc.description.abstract","A rapidly increasing number of RNA helicases are implicated in several distinct cellular processes, however, the modes of regulation of multifunctional RNA helicases and their recruitment to different target complexes have remained unknown. Here, we show that the distribution of the multifunctional DEAH-box RNA helicase Prp43 between its diverse cellular functions can be regulated by the interplay of its G-patch protein cofactors. We identify the orphan G-patch protein Cmg1 (YLR271W) as a novel cofactor of Prp43 and show that it stimulates the RNA binding and ATPase activity of the helicase. Interestingly, Cmg1 localizes to the cytoplasm and to the intermembrane space of mitochondria and its overexpression promotes apoptosis. Furthermore, our data reveal that different G-patch protein cofactors compete for interaction with Prp43. Changes in the expression levels of Prp43-interacting G-patch proteins modulate the cellular localization of Prp43 and G-patch protein overexpression causes accumulation of the helicase in the cytoplasm or nucleoplasm. Overexpression of several G-patch proteins also leads to defects in ribosome biogenesis that are consistent with withdrawal of the helicase from this pathway. Together, these findings suggest that the availability of cofactors and the sequestering of the helicase are means to regulate the activity of multifunctional RNA helicases and their distribution between different cellular processes."],["dc.description.sponsorship","Open-Access Publikationsfonds 2016"],["dc.identifier.doi","10.1080/15476286.2016.1142038"],["dc.identifier.gro","3141714"],["dc.identifier.isi","000372909600008"],["dc.identifier.pmid","26821976"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13404"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/258"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1555-8584"],["dc.relation.issn","1547-6286"],["dc.rights","CC BY-NC 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/3.0"],["dc.title","Protein cofactor competition regulates the action of a multifunctional RNA helicase in different pathways"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.contributor.author","Heininger, Annika"],["dc.date.accessioned","2018-05-03T10:44:51Z"],["dc.date.available","2018-05-03T10:44:51Z"],["dc.date.issued","2016"],["dc.description.abstract","RNA helicases have many important roles in cell metabolism and are involved in numerous pathways, e.g. translation, pre-mRNA splicing and biogenesis. Interestingly, an increasing number of RNA helicases have been shown to be required for more than one cellular pathway. Therefore, protein cofactors have been suggested to recruit multifunctional RNA helicases to their substrates and regulate their activity. The best characterised family of helicase cofactors are G-patch proteins, which all contain a glycine-riche domain. This work focuses on the characterisation of the yeast RNA helicase Prp43 and its G-patch protein cofactors. Additionally, a new G-patch protein cofactor of Prp43 was identified and characterised. Together, the data suggest that protein cofactors can regulate the distribution and activity of RNA helicases in different pathways."],["dc.description.tableofcontents","

• INDEX
• SUMMARY
• 1. INTRODUCTION
• 1.1. RNA helicases
• 1.2. Pre-mRNA splicing
• 1.3. Ribosome biogenesis
• 1.4. G-patch proteins
• 1.5. Aims
• 2. MATERIALS AND METHODS
• 2.1. Materials
• 2.2. Methods
• 3. RESULTS
• 3.1. Identification of Cmg1-interacting helicases
• 3.2. Analysis of the Cmg1 - Prp43 interactionin vitro
• 3.3. Identification of Cmg1 and Prp43interacting domains
• 3.4. Effect of Cmg1 on the RNA binding affinityof Prp43
• 3.5. Prp43 ATPase activity in the presence ofCmg1
• 3.6. Cmg1 cellular localisation
• 3.7. Submitochondrial localisation of Cmg1
• 3.8. Analysis of mitochondrial metabolism uponcmg1 deletion or overexpression
• 3.9. Cell growth and survival in cmg1 deletion and overexpression strains
• 3.10. Relocalisation of Cmg1 and Prp43 underapoptotic conditions
• 3.11. Mitochondrial binding partners of Prp43 inapoptosis
• 3.12. Prp43 localisation in the complex IIIdeficient strain
• 3.13. Localisation of Prp43 upon G-patch proteinoverexpression
• 3.14. G-patch proteins compete for Prp43binding
• 3.15. Overexpression of G-patch proteins affectsprecursor ribosomal RNA processing
• 4. DISCUSSION
• 4.1. Characterisation of the orphan G-patchprotein Cmg1
• 4.2. Prp43 at mitochondria in apoptosis
• 4.3. Recruitment of helicases to their target sites
• 4.4. Regulation of RNA helicases by cofactorcompetition
• 4.5. Conclusions
• 5. REFERENCES
• PUBLICATION
• ACKNOWLEDGMENTS
• CURRICULUM VITAE

"],["dc.format.extent","88"],["dc.identifier.doi","10.17875/gup2016-953"],["dc.identifier.isbn","978-3-86395-237-2"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?univerlag-isbn-978-3-86395-237-2"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/14455"],["dc.identifier.urn","urn:nbn:de:gbv:7-isbn-978-3-86395-237-2-3"],["dc.language.iso","en"],["dc.notes.intern","TASK GROB-550"],["dc.notes.status","zu prüfen"],["dc.publisher","Universitätsverlag Göttingen"],["dc.publisher.place","Göttingen"],["dc.title","Characterisation of the yeast RNA helicase Prp43"],["dc.type","thesis"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]