Literature DB >> 18075577

The origin of protein interactions and allostery in colocalization.

John Kuriyan1, David Eisenberg.   

Abstract

Two fundamental principles can account for how regulated networks of interacting proteins originated in cells. These are the law of mass action, which holds that the binding of one molecule to another increases with concentration, and the fact that the colocalization of molecules vastly increases their local concentrations. It follows that colocalization can amplify the effect on one protein of random mutations in another protein and can therefore, through natural selection, lead to interactions between proteins and to a startling variety of complex allosteric controls. It also follows that allostery is common and that homologous proteins can have different allosteric mechanisms. Thus, the regulated protein networks of organisms seem to be the inevitable consequence of natural selection operating under physical laws.

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Year:  2007        PMID: 18075577     DOI: 10.1038/nature06524

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  165 in total

1.  In vivo application of photocleavable protein interaction reporter technology.

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2.  The evolution of multimeric protein assemblages.

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Journal:  Mol Biol Evol       Date:  2011-12-05       Impact factor: 16.240

3.  Protein misinteraction avoidance causes highly expressed proteins to evolve slowly.

Authors:  Jian-Rong Yang; Ben-Yang Liao; Shi-Mei Zhuang; Jianzhi Zhang
Journal:  Proc Natl Acad Sci U S A       Date:  2012-03-13       Impact factor: 11.205

4.  Quantifying spatial correlations of fluorescent markers using enhanced background reduction with protein proximity index and correlation coefficient estimations.

Authors:  Vadim Zinchuk; Yong Wu; Olga Grossenbacher-Zinchuk; Enrico Stefani
Journal:  Nat Protoc       Date:  2011-09-15       Impact factor: 13.491

5.  Determinants of structural and functional plasticity of a widely conserved protease chaperone complex.

Authors:  Melisa Merdanovic; Nicolette Mamant; Michael Meltzer; Simon Poepsel; Alexandra Auckenthaler; Rie Melgaard; Patrick Hauske; Luitgard Nagel-Steger; Anthony R Clarke; Markus Kaiser; Robert Huber; Michael Ehrmann
Journal:  Nat Struct Mol Biol       Date:  2010-06-27       Impact factor: 15.369

6.  Allosteric response is both conserved and variable across three CheY orthologs.

Authors:  James M Mottonen; Donald J Jacobs; Dennis R Livesay
Journal:  Biophys J       Date:  2010-10-06       Impact factor: 4.033

7.  The Ras G Domain Lacks the Intrinsic Propensity to Form Dimers.

Authors:  Elizaveta A Kovrigina; Azamat R Galiakhmetov; Evgenii L Kovrigin
Journal:  Biophys J       Date:  2015-09-01       Impact factor: 4.033

8.  Substrate and inhibitor-induced dimerization and cooperativity in caspase-1 but not caspase-3.

Authors:  Debajyoti Datta; Christopher L McClendon; Matthew P Jacobson; James A Wells
Journal:  J Biol Chem       Date:  2013-02-05       Impact factor: 5.157

9.  Structural basis for protein antiaggregation activity of the trigger factor chaperone.

Authors:  Tomohide Saio; Xiao Guan; Paolo Rossi; Anastassios Economou; Charalampos G Kalodimos
Journal:  Science       Date:  2014-05-09       Impact factor: 47.728

10.  Assembly of the Sos1-Grb2-Gab1 ternary signaling complex is under allosteric control.

Authors:  Caleb B McDonald; Kenneth L Seldeen; Brian J Deegan; Vikas Bhat; Amjad Farooq
Journal:  Arch Biochem Biophys       Date:  2009-12-22       Impact factor: 4.013

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