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Human Translation Initiation Factor eIF4G1 Possesses a Low-Affinity ATP Binding Site Facing the ATP-Binding Cleft of eIF4A in the eIF4G/eIF4A Complex
[Image: see text] Eukaryotic translation initiation factor 4G (eIF4G) plays a crucial role in translation initiation, serving as a scaffolding protein binding several other initiation factors, other proteins, and RNA. Binding of eIF4G to the ATP-dependent RNA helicase eukaryotic translation initiati...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2014
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4204880/ https://www.ncbi.nlm.nih.gov/pubmed/25255371 http://dx.doi.org/10.1021/bi500600m |
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author | Akabayov, Sabine R. Akabayov, Barak Wagner, Gerhard |
author_facet | Akabayov, Sabine R. Akabayov, Barak Wagner, Gerhard |
author_sort | Akabayov, Sabine R. |
collection | PubMed |
description | [Image: see text] Eukaryotic translation initiation factor 4G (eIF4G) plays a crucial role in translation initiation, serving as a scaffolding protein binding several other initiation factors, other proteins, and RNA. Binding of eIF4G to the ATP-dependent RNA helicase eukaryotic translation initiation factor 4A (eIF4A) enhances the activity of eIF4A in solution and in crowded environments. Previously, this activity enhancement was solely attributed to eIF4G, conferring a closed, active conformation upon eIF4A. Here we show that eIF4G contains a low-affinity binding site at the entrance to the ATP-binding cleft on eIF4A, suggesting that regulation of the local ATP concentration may be an additional reason for the enhancement in activity. |
format | Online Article Text |
id | pubmed-4204880 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | American
Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-42048802015-09-25 Human Translation Initiation Factor eIF4G1 Possesses a Low-Affinity ATP Binding Site Facing the ATP-Binding Cleft of eIF4A in the eIF4G/eIF4A Complex Akabayov, Sabine R. Akabayov, Barak Wagner, Gerhard Biochemistry [Image: see text] Eukaryotic translation initiation factor 4G (eIF4G) plays a crucial role in translation initiation, serving as a scaffolding protein binding several other initiation factors, other proteins, and RNA. Binding of eIF4G to the ATP-dependent RNA helicase eukaryotic translation initiation factor 4A (eIF4A) enhances the activity of eIF4A in solution and in crowded environments. Previously, this activity enhancement was solely attributed to eIF4G, conferring a closed, active conformation upon eIF4A. Here we show that eIF4G contains a low-affinity binding site at the entrance to the ATP-binding cleft on eIF4A, suggesting that regulation of the local ATP concentration may be an additional reason for the enhancement in activity. American Chemical Society 2014-09-25 2014-10-21 /pmc/articles/PMC4204880/ /pubmed/25255371 http://dx.doi.org/10.1021/bi500600m Text en Copyright © 2014 American Chemical Society Terms of Use (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) |
spellingShingle | Akabayov, Sabine R. Akabayov, Barak Wagner, Gerhard Human Translation Initiation Factor eIF4G1 Possesses a Low-Affinity ATP Binding Site Facing the ATP-Binding Cleft of eIF4A in the eIF4G/eIF4A Complex |
title | Human Translation Initiation
Factor eIF4G1 Possesses
a Low-Affinity ATP Binding Site Facing the ATP-Binding Cleft of eIF4A
in the eIF4G/eIF4A Complex |
title_full | Human Translation Initiation
Factor eIF4G1 Possesses
a Low-Affinity ATP Binding Site Facing the ATP-Binding Cleft of eIF4A
in the eIF4G/eIF4A Complex |
title_fullStr | Human Translation Initiation
Factor eIF4G1 Possesses
a Low-Affinity ATP Binding Site Facing the ATP-Binding Cleft of eIF4A
in the eIF4G/eIF4A Complex |
title_full_unstemmed | Human Translation Initiation
Factor eIF4G1 Possesses
a Low-Affinity ATP Binding Site Facing the ATP-Binding Cleft of eIF4A
in the eIF4G/eIF4A Complex |
title_short | Human Translation Initiation
Factor eIF4G1 Possesses
a Low-Affinity ATP Binding Site Facing the ATP-Binding Cleft of eIF4A
in the eIF4G/eIF4A Complex |
title_sort | human translation initiation
factor eif4g1 possesses
a low-affinity atp binding site facing the atp-binding cleft of eif4a
in the eif4g/eif4a complex |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4204880/ https://www.ncbi.nlm.nih.gov/pubmed/25255371 http://dx.doi.org/10.1021/bi500600m |
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