Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation.
The production of a functional mRNA is regulated at every step of transcription. An area not well-understood is the transition of RNA polymerase II from elongation to termination. The S. cerevisiae SR-like protein Npl3 functions to negatively regulate transcription termination by antagonizing the bi...
| Main Authors: | , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2008-09-01
|
| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC2538588?pdf=render |
| _version_ | 1819057404626599936 |
|---|---|
| author | Jessica L Dermody Jonathan M Dreyfuss Judit Villén Babatunde Ogundipe Steven P Gygi Peter J Park Alfred S Ponticelli Claire L Moore Stephen Buratowski Miriam E Bucheli |
| author_facet | Jessica L Dermody Jonathan M Dreyfuss Judit Villén Babatunde Ogundipe Steven P Gygi Peter J Park Alfred S Ponticelli Claire L Moore Stephen Buratowski Miriam E Bucheli |
| author_sort | Jessica L Dermody |
| collection | DOAJ |
| description | The production of a functional mRNA is regulated at every step of transcription. An area not well-understood is the transition of RNA polymerase II from elongation to termination. The S. cerevisiae SR-like protein Npl3 functions to negatively regulate transcription termination by antagonizing the binding of polyA/termination proteins to the mRNA. In this study, Npl3 is shown to interact with the CTD and have a direct stimulatory effect on the elongation activity of the polymerase. The interaction is inhibited by phosphorylation of Npl3. In addition, Casein Kinase 2 was found to be required for the phosphorylation of Npl3 and affect its ability to compete against Rna15 (Cleavage Factor I) for binding to polyA signals. Our results suggest that phosphorylation of Npl3 promotes its dissociation from the mRNA/RNAP II, and contributes to the association of the polyA/termination factor Rna15. This work defines a novel role for Npl3 in elongation and its regulation by phosphorylation. |
| first_indexed | 2024-12-21T13:38:46Z |
| format | Article |
| id | doaj.art-e7cc1d51db8c434ebda3c455aa7743c1 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-21T13:38:46Z |
| publishDate | 2008-09-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-e7cc1d51db8c434ebda3c455aa7743c12022-12-21T19:02:06ZengPublic Library of Science (PLoS)PLoS ONE1932-62032008-09-0139e327310.1371/journal.pone.0003273Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation.Jessica L DermodyJonathan M DreyfussJudit VillénBabatunde OgundipeSteven P GygiPeter J ParkAlfred S PonticelliClaire L MooreStephen BuratowskiMiriam E BucheliThe production of a functional mRNA is regulated at every step of transcription. An area not well-understood is the transition of RNA polymerase II from elongation to termination. The S. cerevisiae SR-like protein Npl3 functions to negatively regulate transcription termination by antagonizing the binding of polyA/termination proteins to the mRNA. In this study, Npl3 is shown to interact with the CTD and have a direct stimulatory effect on the elongation activity of the polymerase. The interaction is inhibited by phosphorylation of Npl3. In addition, Casein Kinase 2 was found to be required for the phosphorylation of Npl3 and affect its ability to compete against Rna15 (Cleavage Factor I) for binding to polyA signals. Our results suggest that phosphorylation of Npl3 promotes its dissociation from the mRNA/RNAP II, and contributes to the association of the polyA/termination factor Rna15. This work defines a novel role for Npl3 in elongation and its regulation by phosphorylation.http://europepmc.org/articles/PMC2538588?pdf=render |
| spellingShingle | Jessica L Dermody Jonathan M Dreyfuss Judit Villén Babatunde Ogundipe Steven P Gygi Peter J Park Alfred S Ponticelli Claire L Moore Stephen Buratowski Miriam E Bucheli Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation. PLoS ONE |
| title | Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation. |
| title_full | Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation. |
| title_fullStr | Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation. |
| title_full_unstemmed | Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation. |
| title_short | Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation. |
| title_sort | unphosphorylated sr like protein npl3 stimulates rna polymerase ii elongation |
| url | http://europepmc.org/articles/PMC2538588?pdf=render |
| work_keys_str_mv | AT jessicaldermody unphosphorylatedsrlikeproteinnpl3stimulatesrnapolymeraseiielongation AT jonathanmdreyfuss unphosphorylatedsrlikeproteinnpl3stimulatesrnapolymeraseiielongation AT juditvillen unphosphorylatedsrlikeproteinnpl3stimulatesrnapolymeraseiielongation AT babatundeogundipe unphosphorylatedsrlikeproteinnpl3stimulatesrnapolymeraseiielongation AT stevenpgygi unphosphorylatedsrlikeproteinnpl3stimulatesrnapolymeraseiielongation AT peterjpark unphosphorylatedsrlikeproteinnpl3stimulatesrnapolymeraseiielongation AT alfredsponticelli unphosphorylatedsrlikeproteinnpl3stimulatesrnapolymeraseiielongation AT clairelmoore unphosphorylatedsrlikeproteinnpl3stimulatesrnapolymeraseiielongation AT stephenburatowski unphosphorylatedsrlikeproteinnpl3stimulatesrnapolymeraseiielongation AT miriamebucheli unphosphorylatedsrlikeproteinnpl3stimulatesrnapolymeraseiielongation |