2009
DOI: 10.1073/pnas.0902251106
|View full text |Cite
|
Sign up to set email alerts
|

Structure of the C-terminus of the mRNA export factor Dbp5 reveals the interaction surface for the ATPase activator Gle1

Abstract: The DExD/H-box RNA-dependent ATPase Dbp5 plays an essential role in the nuclear export of mRNA. Dbp5 localizes to the nuclear pore complex, where its ATPase activity is stimulated by Gle1 and its coactivator inositol hexakisphosphate. Here, we present the crystal structure of the C-terminal domain of Dbp5, refined to 1.8 Å. The structure reveals a RecA-like fold that contains two defining characteristics not present in other structurally characterized DExD/H-box proteins: a C-terminal ␣-helix and a loop connec… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

6
41
0

Year Published

2010
2010
2022
2022

Publication Types

Select...
7
1

Relationship

0
8

Authors

Journals

citations
Cited by 34 publications
(47 citation statements)
references
References 40 publications
6
41
0
Order By: Relevance
“…2E). These results suggest that a threshold of Dbp5 activity might be required for viability, consistent with another recent report analyzing dbp5 mutants (26).…”
Section: Conserved Gle1 Residues Lyssupporting
confidence: 81%
See 2 more Smart Citations
“…2E). These results suggest that a threshold of Dbp5 activity might be required for viability, consistent with another recent report analyzing dbp5 mutants (26).…”
Section: Conserved Gle1 Residues Lyssupporting
confidence: 81%
“…Sequence analysis reveals a highly conserved C-terminal domain and a more divergent N-terminal domain (18). Interestingly, the conserved C-terminal domain of Gle1 is responsible for interaction with the conserved mRNA export factor Dbp5 (20,22,24,26).…”
mentioning
confidence: 99%
See 1 more Smart Citation
“…[22][23][24][25][26] The apo form of Dbp5 adopts an open extended conformation with no interaction between its two RecA-like domains (Fig. 1A), 25 consistent with the results obtained by small-angle X-ray scattering (SAXS).…”
Section: Structural Insights Into Dbp5's Function In Mrna Exportsupporting
confidence: 77%
“…Dbp5 exhibits quite low ATPase activity on its own. Gle1 and IP6 activate the ATPase activity of Dbp5 (Dossani et al, 2009;Weirich et al, 2006). Recently, the Dbp5-Gle1 and IP6 complex was shown to be structurally similar to the eIF4A-eIF4G complex which is essential for translation initiation.…”
Section: The Role Of Dbp5-gle1 and Ip6 In The Release Of Mrna Into Thmentioning
confidence: 99%