MLN51 stimulates the RNA-helicase activity of eIF4AIII.
The core of the exon-junction complex consists of Y14, Magoh, MLN51 and eIF4AIII, a DEAD-box RNA helicase. MLN51 stimulates the ATPase activity of eIF4AIII, whilst the Y14-Magoh complex inhibits it. We show that the MLN51-dependent stimulation increases both the affinity of eIF4AIII for ATP and the...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2007-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC1810427?pdf=render |
| _version_ | 1828782672710729728 |
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| author | Christian G Noble Haiwei Song |
| author_facet | Christian G Noble Haiwei Song |
| author_sort | Christian G Noble |
| collection | DOAJ |
| description | The core of the exon-junction complex consists of Y14, Magoh, MLN51 and eIF4AIII, a DEAD-box RNA helicase. MLN51 stimulates the ATPase activity of eIF4AIII, whilst the Y14-Magoh complex inhibits it. We show that the MLN51-dependent stimulation increases both the affinity of eIF4AIII for ATP and the rate of enzyme turnover; the K(M) is decreased by an order of magnitude and k(cat) increases 30 fold. Y14-Magoh do inhibit the MLN51-stimulated ATPase activity, but not back to background levels. The ATP-bound form of the eIF4AIII-MLN51 complex has a 100-fold higher affinity for RNA than the unbound form and ATP hydrolysis reduces this affinity. MLN51 stimulates the RNA-helicase activity of eIF4AIII, suggesting that this activity may be functionally important. |
| first_indexed | 2024-12-11T17:53:10Z |
| format | Article |
| id | doaj.art-ddaa417b592d438f88f5c6c3082fd144 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-11T17:53:10Z |
| publishDate | 2007-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-ddaa417b592d438f88f5c6c3082fd1442022-12-22T00:56:09ZengPublic Library of Science (PLoS)PLoS ONE1932-62032007-01-0123e30310.1371/journal.pone.0000303MLN51 stimulates the RNA-helicase activity of eIF4AIII.Christian G NobleHaiwei SongThe core of the exon-junction complex consists of Y14, Magoh, MLN51 and eIF4AIII, a DEAD-box RNA helicase. MLN51 stimulates the ATPase activity of eIF4AIII, whilst the Y14-Magoh complex inhibits it. We show that the MLN51-dependent stimulation increases both the affinity of eIF4AIII for ATP and the rate of enzyme turnover; the K(M) is decreased by an order of magnitude and k(cat) increases 30 fold. Y14-Magoh do inhibit the MLN51-stimulated ATPase activity, but not back to background levels. The ATP-bound form of the eIF4AIII-MLN51 complex has a 100-fold higher affinity for RNA than the unbound form and ATP hydrolysis reduces this affinity. MLN51 stimulates the RNA-helicase activity of eIF4AIII, suggesting that this activity may be functionally important.http://europepmc.org/articles/PMC1810427?pdf=render |
| spellingShingle | Christian G Noble Haiwei Song MLN51 stimulates the RNA-helicase activity of eIF4AIII. PLoS ONE |
| title | MLN51 stimulates the RNA-helicase activity of eIF4AIII. |
| title_full | MLN51 stimulates the RNA-helicase activity of eIF4AIII. |
| title_fullStr | MLN51 stimulates the RNA-helicase activity of eIF4AIII. |
| title_full_unstemmed | MLN51 stimulates the RNA-helicase activity of eIF4AIII. |
| title_short | MLN51 stimulates the RNA-helicase activity of eIF4AIII. |
| title_sort | mln51 stimulates the rna helicase activity of eif4aiii |
| url | http://europepmc.org/articles/PMC1810427?pdf=render |
| work_keys_str_mv | AT christiangnoble mln51stimulatesthernahelicaseactivityofeif4aiii AT haiweisong mln51stimulatesthernahelicaseactivityofeif4aiii |