Literature DB >> 22750478

The cation-dependent G-proteins: in a class of their own.

Miriam-Rose Ash1, Megan J Maher, J Mitchell Guss, Mika Jormakka.   

Abstract

G-proteins are some of the most important and abundant enzymes, yet their intrinsic nucleotide hydrolysis reaction is notoriously slow and must be accelerated in vivo. Recent experiments on dynamin and GTPases involved in ribosome assembly have demonstrated that their hydrolysis activities are stimulated by potassium ions. This article presents the hypothesis that cation-mediated activation of G-proteins is more common than currently realised, and that such GTPases represent a structurally and functionally unique class of G-proteins. Based on sequence analysis we provide a list of predicted cation-dependent GTPases, which encompasses almost all members of the TEES, Obg-HflX, YqeH-like and dynamin superfamilies. The results from this analysis effectively re-define the conditions under which many of these G-proteins should be studied in vitro.
Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Year:  2012        PMID: 22750478     DOI: 10.1016/j.febslet.2012.06.030

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  20 in total

Review 1.  Building a fission machine--structural insights into dynamin assembly and activation.

Authors:  Joshua S Chappie; Fred Dyda
Journal:  J Cell Sci       Date:  2013-06-18       Impact factor: 5.285

2.  Structural and biochemical analysis of Escherichia coli ObgE, a central regulator of bacterial persistence.

Authors:  Sotirios Gkekas; Ranjan Kumar Singh; Alexander V Shkumatov; Joris Messens; Maarten Fauvart; Natalie Verstraeten; Jan Michiels; Wim Versées
Journal:  J Biol Chem       Date:  2017-02-21       Impact factor: 5.157

3.  Nmd3 is a structural mimic of eIF5A, and activates the cpGTPase Lsg1 during 60S ribosome biogenesis.

Authors:  Andrey G Malyutin; Sharmishtha Musalgaonkar; Stephanie Patchett; Joachim Frank; Arlen W Johnson
Journal:  EMBO J       Date:  2017-02-08       Impact factor: 11.598

4.  A monovalent cation acts as structural and catalytic cofactor in translational GTPases.

Authors:  Bernhard Kuhle; Ralf Ficner
Journal:  EMBO J       Date:  2014-09-15       Impact factor: 11.598

5.  Structure of an atypical FeoB G-domain reveals a putative domain-swapped dimer.

Authors:  Chandrika N Deshpande; Aaron P McGrath; Josep Font; Amy P Guilfoyle; Megan J Maher; Mika Jormakka
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2013-03-29

6.  Ancient Systems of Sodium/Potassium Homeostasis as Predecessors of Membrane Bioenergetics.

Authors:  D V Dibrova; M Y Galperin; E V Koonin; A Y Mulkidjanian
Journal:  Biochemistry (Mosc)       Date:  2015-05       Impact factor: 2.487

7.  Evolution of cation binding in the active sites of P-loop nucleoside triphosphatases in relation to the basic catalytic mechanism.

Authors:  Daria N Shalaeva; Dmitry A Cherepanov; Michael Y Galperin; Andrey V Golovin; Armen Y Mulkidjanian
Journal:  Elife       Date:  2018-12-11       Impact factor: 8.140

8.  Ribosome-induced tuning of GTP hydrolysis by a translational GTPase.

Authors:  Cristina Maracci; Frank Peske; Ev Dannies; Corinna Pohl; Marina V Rodnina
Journal:  Proc Natl Acad Sci U S A       Date:  2014-09-22       Impact factor: 11.205

9.  The tRNA-modifying function of MnmE is controlled by post-hydrolysis steps of its GTPase cycle.

Authors:  Silvia Prado; Magda Villarroya; Milagros Medina; M-Eugenia Armengod
Journal:  Nucleic Acids Res       Date:  2013-04-28       Impact factor: 16.971

10.  Coupled GTPase and remodelling ATPase activities form a checkpoint for ribosome export.

Authors:  Sander Granneman; Matthias Thoms; Yoshitaka Matsuo; Rizos-Georgios Manikas; David Tollervey; Ed Hurt
Journal:  Nature       Date:  2013-11-17       Impact factor: 49.962

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