1jhs

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(New page: 200px<br /><applet load="1jhs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jhs, resolution 1.90&Aring;" /> '''Protein Mog1 E65A mu...)
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[[Image:1jhs.jpg|left|200px]]<br /><applet load="1jhs" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jhs.jpg|left|200px]]<br /><applet load="1jhs" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jhs, resolution 1.90&Aring;" />
caption="1jhs, resolution 1.90&Aring;" />
'''Protein Mog1 E65A mutant'''<br />
'''Protein Mog1 E65A mutant'''<br />
==Overview==
==Overview==
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Mog1 is a nuclear protein that interacts with Ran, the Ras family GTPase, that confers directionality to nuclear import and export pathways., Deletion of MOG1 in Saccharomyces cerevisiae (Deltamog1) causes, temperature-sensitive growth and defects in nuclear protein import. Mog1, has previously been shown to stimulate GTP release from Ran and we, demonstrate here that addition of Mog1 to either Ran-GTP or Ran-GDP, results in nucleotide release and formation of a stable complex between, Mog1 and nucleotide-free Ran. Moreover, MOG1 shows synthetic lethality, with PRP20, the Ran guanine nucleotide exchange factor (RanGEF) that also, binds nucleotide-free Ran. To probe the functional role of the Mog1-Ran, interaction, we engineered mutants of yeast Mog1 and Ran that specifically, disrupt their interaction both in vitro and in vivo. These mutants, indicate that the interaction interface involves conserved Mog1p residues, Asp(62) and Glu(65), and residue Lys(136) in yeast Ran. Mutations at these, residues decrease the ability of Mog1 to bind and release nucleotide from, Ran. Furthermore, the E65K-Mog1 and K136E-Ran mutations in yeast cause, temperature sensitivity and mislocalization of a nuclear import reporter, protein, similar to the phenotype observed for the Deltamog1 strain. Our, results indicate that a primary function of Mog1 requires binding to Ran, and that the Mog1-Ran interaction is necessary for efficient nuclear, protein import in vivo.
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Mog1 is a nuclear protein that interacts with Ran, the Ras family GTPase that confers directionality to nuclear import and export pathways. Deletion of MOG1 in Saccharomyces cerevisiae (Deltamog1) causes temperature-sensitive growth and defects in nuclear protein import. Mog1 has previously been shown to stimulate GTP release from Ran and we demonstrate here that addition of Mog1 to either Ran-GTP or Ran-GDP results in nucleotide release and formation of a stable complex between Mog1 and nucleotide-free Ran. Moreover, MOG1 shows synthetic lethality with PRP20, the Ran guanine nucleotide exchange factor (RanGEF) that also binds nucleotide-free Ran. To probe the functional role of the Mog1-Ran interaction, we engineered mutants of yeast Mog1 and Ran that specifically disrupt their interaction both in vitro and in vivo. These mutants indicate that the interaction interface involves conserved Mog1p residues Asp(62) and Glu(65), and residue Lys(136) in yeast Ran. Mutations at these residues decrease the ability of Mog1 to bind and release nucleotide from Ran. Furthermore, the E65K-Mog1 and K136E-Ran mutations in yeast cause temperature sensitivity and mislocalization of a nuclear import reporter protein, similar to the phenotype observed for the Deltamog1 strain. Our results indicate that a primary function of Mog1 requires binding to Ran and that the Mog1-Ran interaction is necessary for efficient nuclear protein import in vivo.
==About this Structure==
==About this Structure==
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1JHS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JHS OCA].
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1JHS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JHS OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Baker, R.P.]]
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[[Category: Baker, R P.]]
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[[Category: Corbett, A.H.]]
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[[Category: Corbett, A H.]]
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[[Category: Ecclestone, J.F.]]
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[[Category: Ecclestone, J F.]]
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[[Category: Harreman, M.T.]]
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[[Category: Harreman, M T.]]
[[Category: Stewart, M.]]
[[Category: Stewart, M.]]
[[Category: gsp1]]
[[Category: gsp1]]
[[Category: nuclear-protein import]]
[[Category: nuclear-protein import]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:16:21 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:22:50 2008''

Revision as of 11:22, 21 February 2008


1jhs, resolution 1.90Å

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Protein Mog1 E65A mutant

Overview

Mog1 is a nuclear protein that interacts with Ran, the Ras family GTPase that confers directionality to nuclear import and export pathways. Deletion of MOG1 in Saccharomyces cerevisiae (Deltamog1) causes temperature-sensitive growth and defects in nuclear protein import. Mog1 has previously been shown to stimulate GTP release from Ran and we demonstrate here that addition of Mog1 to either Ran-GTP or Ran-GDP results in nucleotide release and formation of a stable complex between Mog1 and nucleotide-free Ran. Moreover, MOG1 shows synthetic lethality with PRP20, the Ran guanine nucleotide exchange factor (RanGEF) that also binds nucleotide-free Ran. To probe the functional role of the Mog1-Ran interaction, we engineered mutants of yeast Mog1 and Ran that specifically disrupt their interaction both in vitro and in vivo. These mutants indicate that the interaction interface involves conserved Mog1p residues Asp(62) and Glu(65), and residue Lys(136) in yeast Ran. Mutations at these residues decrease the ability of Mog1 to bind and release nucleotide from Ran. Furthermore, the E65K-Mog1 and K136E-Ran mutations in yeast cause temperature sensitivity and mislocalization of a nuclear import reporter protein, similar to the phenotype observed for the Deltamog1 strain. Our results indicate that a primary function of Mog1 requires binding to Ran and that the Mog1-Ran interaction is necessary for efficient nuclear protein import in vivo.

About this Structure

1JHS is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Interaction between Ran and Mog1 is required for efficient nuclear protein import., Baker RP, Harreman MT, Eccleston JF, Corbett AH, Stewart M, J Biol Chem. 2001 Nov 2;276(44):41255-62. Epub 2001 Aug 16. PMID:11509570

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