Functional analysis of the GTPases EngA and YhbZ encoded by Salmonella typhimurium.

Functional analysis of the GTPases EngA and YhbZ encoded by Salmonella typhimurium. Research Abstract Details 

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Functional analysis of the GTPases EngA and YhbZ encoded by Salmonella typhimurium. Abstract Text:

Heather K Lamb,Paul Thompson,Catherine Elliott,Ian G Charles,Jamie Richards,Michael Lockyer,Nicholas Watkins,Charles Nichols,David K Stammers,Clive R Bagshaw,Alan Cooper,Alastair R Hawkins,Heather K Lamb,Paul Thompson,Catherine Elliott,Ian G Charles,Jamie Richards,Michael Lockyer,Nicholas Watkins,Charles Nichols,David K Stammers,Clive R Bagshaw,Alan Cooper,Alastair R Hawkins,

The S. typhimurium genome encodes proteins, designated EngA and YhbZ, which have a high sequence identity with the GTPases EngA/Der and ObgE/CgtAE of Escherichia coli. The wild-type activity of the E. coli proteins is essential for normal ribosome maturation and cell viability. In order to characterize the potential involvement of the Salmonella typhimurium EngA and YhbZ proteins in ribosome biology, we used high stringency affinity chromatography experiments to identify strongly binding ribosomal partner proteins. A combination of biochemical and microcalorimetric analysis was then used to characterize these protein:protein interactions and quantify nucleotide binding affinities. These experiments show that YhbZ specifically interacts with the pseudouridine synthase RluD (KD=2 microM and 1:1 stoichiometry), and we show for the first time that EngA can interact with the ribosomal structural protein S7. Thermodynamic analysis shows both EngA and YhbZ bind GDP with a higher affinity than GTP (20-fold difference for EngA and 3.8-fold for YhbZ), and that the two nucleotide binding sites in EngA show a 5.3-fold difference in affinity for GDP. We report a fluorescence assay for nucleotide binding to EngA and YhbZ, which is suitable for identifying inhibitors specific for this ligand-binding site, which would potentially inhibit their biological functions. The interactions of YhbZ with ribosome structural proteins that we identify may demonstrate a previously unreported additional function for this class of GTPase: that of ensuring delivery of rRNA modifying enzymes to the appropriate region of the ribosome.

Functional analysis of the GTPases EngA and YhbZ encoded by Salmonella typhimurium. Publishing Authors By Initials

HK Lamb,P Thompson,C Elliott,IG Charles,J Richards,M Lockyer,N Watkins,C Nichols,DK Stammers,CR Bagshaw,A Cooper,AR Hawkins,HK Lamb,P Thompson,C Elliott,IG Charles,J Richards,M Lockyer,N Watkins,C Nichols,DK Stammers,CR Bagshaw,A Cooper,AR Hawkins,

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Functional analysis of the GTPases EngA and YhbZ encoded by Salmonella typhimurium. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Protein science : a publication of the Protein Soc

VOLUME: 16

Page Numbers: 2391-402

Journal Abbreviation: Protein Sci.

ISSN: 0961-8368

DAY: 28

MONTH: 09

YEAR: 2007

Functional analysis of the GTPases EngA and YhbZ encoded by Salmonella typhimurium. Information

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LANGUAGE: eng

NlmUniqueID: 9211750

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Grant and Affiliation Information for Functional analysis of the GTPases EngA and YhbZ encoded by Salmonella typhimurium.

AFFILIATION: Institute of Cell and Molecular Biosciences, Medical School, Newcastle University, Newcastle upon Tyne, UK.

Country: United States

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MEDLINETA: Protein Sci

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