Proteins Rpr2 and Pop3 increase the activity and thermal stability of yeast RNase P
RNA-based enzyme RNase P is a ribonucleoprotein complex responsible primarily for 5’-maturation of tRNAs. S. cerevisiae RNase P comprises a catalytic RNA component and nine proteins. The assembly and maturation of S. cerevisiae RNase P involves an abundant and catalytically active precursor form, wh...
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Taylor & Francis Group
2023-12-01
|
| Series: | RNA Biology |
| Subjects: | |
| Online Access: | http://dx.doi.org/10.1080/15476286.2023.2201110 |
| _version_ | 1797403999634194432 |
|---|---|
| author | Anna Perederina Igor Berezin Andrey S. Krasilnikov |
| author_facet | Anna Perederina Igor Berezin Andrey S. Krasilnikov |
| author_sort | Anna Perederina |
| collection | DOAJ |
| description | RNA-based enzyme RNase P is a ribonucleoprotein complex responsible primarily for 5’-maturation of tRNAs. S. cerevisiae RNase P comprises a catalytic RNA component and nine proteins. The assembly and maturation of S. cerevisiae RNase P involves an abundant and catalytically active precursor form, which includes all components except for proteins Rpr2 and Pop3. Rpr2 and Pop3 are essential proteins, but their roles in RNase P were not clear. Here we use a step-wise in vitro assembly of yeast RNase P to show that the addition of proteins Rpr2 and Pop3 increases the activity and thermal stability of the RNase P complex, similar to the effects previously observed for archaeal RNases P. |
| first_indexed | 2024-03-09T02:46:45Z |
| format | Article |
| id | doaj.art-d15839fc218640a68df0877851de88aa |
| institution | Directory Open Access Journal |
| issn | 1547-6286 1555-8584 |
| language | English |
| last_indexed | 2024-03-09T02:46:45Z |
| publishDate | 2023-12-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | RNA Biology |
| spelling | doaj.art-d15839fc218640a68df0877851de88aa2023-12-05T16:09:52ZengTaylor & Francis GroupRNA Biology1547-62861555-85842023-12-0120114915310.1080/15476286.2023.22011102201110Proteins Rpr2 and Pop3 increase the activity and thermal stability of yeast RNase PAnna Perederina0Igor Berezin1Andrey S. Krasilnikov2Pennsylvania State UniversityPennsylvania State UniversityPennsylvania State UniversityRNA-based enzyme RNase P is a ribonucleoprotein complex responsible primarily for 5’-maturation of tRNAs. S. cerevisiae RNase P comprises a catalytic RNA component and nine proteins. The assembly and maturation of S. cerevisiae RNase P involves an abundant and catalytically active precursor form, which includes all components except for proteins Rpr2 and Pop3. Rpr2 and Pop3 are essential proteins, but their roles in RNase P were not clear. Here we use a step-wise in vitro assembly of yeast RNase P to show that the addition of proteins Rpr2 and Pop3 increases the activity and thermal stability of the RNase P complex, similar to the effects previously observed for archaeal RNases P.http://dx.doi.org/10.1080/15476286.2023.2201110ribonuclease prnase pribonucleoproteinrnpyeast |
| spellingShingle | Anna Perederina Igor Berezin Andrey S. Krasilnikov Proteins Rpr2 and Pop3 increase the activity and thermal stability of yeast RNase P RNA Biology ribonuclease p rnase p ribonucleoprotein rnp yeast |
| title | Proteins Rpr2 and Pop3 increase the activity and thermal stability of yeast RNase P |
| title_full | Proteins Rpr2 and Pop3 increase the activity and thermal stability of yeast RNase P |
| title_fullStr | Proteins Rpr2 and Pop3 increase the activity and thermal stability of yeast RNase P |
| title_full_unstemmed | Proteins Rpr2 and Pop3 increase the activity and thermal stability of yeast RNase P |
| title_short | Proteins Rpr2 and Pop3 increase the activity and thermal stability of yeast RNase P |
| title_sort | proteins rpr2 and pop3 increase the activity and thermal stability of yeast rnase p |
| topic | ribonuclease p rnase p ribonucleoprotein rnp yeast |
| url | http://dx.doi.org/10.1080/15476286.2023.2201110 |
| work_keys_str_mv | AT annaperederina proteinsrpr2andpop3increasetheactivityandthermalstabilityofyeastrnasep AT igorberezin proteinsrpr2andpop3increasetheactivityandthermalstabilityofyeastrnasep AT andreyskrasilnikov proteinsrpr2andpop3increasetheactivityandthermalstabilityofyeastrnasep |