Please use this identifier to cite or link to this item:
https://olympias.lib.uoi.gr/jspui/handle/123456789/10453Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Stamatopoulou, V. | en |
| dc.contributor.author | Toumpeki, C. | en |
| dc.contributor.author | Tzakos, A. | en |
| dc.contributor.author | Vourekas, A. | en |
| dc.contributor.author | Drainas, D. | en |
| dc.date.accessioned | 2015-11-24T16:56:34Z | - |
| dc.date.available | 2015-11-24T16:56:34Z | - |
| dc.identifier.issn | 0006-2960 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/10453 | - |
| dc.rights | Default Licence | - |
| dc.subject | pyrococcus-horikoshii ot3 | en |
| dc.subject | archaeal ribonuclease-p | en |
| dc.subject | crystal-structure | en |
| dc.subject | functional reconstitution | en |
| dc.subject | processing enzyme | en |
| dc.subject | furiosus rpp21 | en |
| dc.subject | noncoding rnas | en |
| dc.subject | mrp rna | en |
| dc.subject | holoenzyme | en |
| dc.subject | homolog | en |
| dc.title | Domain Architecture of the DRpp29 Protein and Its interaction with the RNA Subunit of Dictyostelium discoideum RNase P | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | Doi 10.1021/Bi101297z | - |
| heal.identifier.secondary | <Go to ISI>://000285216500015 | - |
| heal.identifier.secondary | http://pubs.acs.org/doi/pdfplus/10.1021/bi101297z | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 2010 | - |
| heal.abstract | Dictyostelium discoideum nuclear RNase P is a ribonucleoprotein complex that displays similarities with its counterparts from higher eukaryotes such as the human enzyme, but at the same time it retains distinctive characteristics. In the present study, we report the molecular cloning and interaction details of DRpp29 and RNase P RNA, two subunits of the RNase P holoenzyme from D. discoideum. Electrophoretic mobility shift assays exhibited that DRpp29 binds specifically to the RNase P RNA subunit, a feature that was further confirmed by the molecular modeling of the DRpp29 structure. Moreover, deletion mutants of DRpp29 were constructed in order to investigate the domains of DRpp29 that contribute to and/or are responsible for the direct interaction with the D. discoidewn RNase P RNA. A eukaryotic specific, lysine- and arginine-rich region was revealed, which seems to facilitate the interaction between these two subunits. Furthermore, we tested the ability of wild-type and mutant DRpp29 to form active RNase P enzymatic particles with the Escherichia coli RNase P RNA. | en |
| heal.publisher | American Chemical Society | en |
| heal.journalName | Biochemistry | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Stamatopoulou-2010-Domain Architecture.pdf | 1.32 MB | Adobe PDF | View/Open Request a copy |
This item is licensed under a Creative Commons License
