ArticleNucleic acids research2009
Distinct GDP/GTP bound states of the tandem G-domains of EngA regulate ribosome binding.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 37 citations in OpenAlex.
- Characterizing a novel CMK-EngA fusion protein fromBiochemistry and biophysics reports · 2023Article
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- Structural insights into the function of a unique tandem GTPase EngA in bacterial ribosome assembly.Nucleic acids research · 2014Article
- A genome-scale metabolic flux model of Escherichia coli K-12 derived from the EcoCyc database.BMC systems biology · 2014Article
- Phenotypic investigations of the depletion of EngA in Escherichia coli are consistent with a role in ribosome biogenesis.FEMS microbiology letters · 2014Article
- Identification and characterization of a hitherto unknown nucleotide-binding domain and an intricate interdomain regulation in HflX-a ribosome binding GTPase.Nucleic acids research · 2013Article
- The tRNAarg gene and engA are essential genes on the 1.7-Mb pSymB megaplasmid of Sinorhizobium meliloti and were translocated together from the chromosome in an ancestral strain.Journal of bacteriology · 2013Article
- Extended C-terminus and length of the linker connecting the G-domains are species-specific variations in the EngA family of GTPases.FEBS open bio · 2012Article
- Exploring potassium-dependent GTP hydrolysis in TEES family GTPases.FEBS open bio · 2012Article
- Potassium acts as a GTPase-activating element on each nucleotide-binding domain of the essential Bacillus subtilis EngA.PloS one · 2012Article
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- The universally conserved prokaryotic GTPases.Microbiology and molecular biology reviews : MMBR · 2011Review
- Megadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry, and hierarchical clustering.Molecular & cellular proteomics : MCP · 2010Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
EngA, a unique GTPase containing a KH-domain preceded by two consecutive G-domains, displays distinct nucleotide binding and hydrolysis activities. So far, Escherichia coli EngA is reported to bind the 50S ribosomal subunit in the guanosine-5'-trihosphate (GTP) bound state. Here, for the first time, using mutations that allow isolating the activities of the two G-domains, GD1 and GD2, we show that apart from 50S, EngA also binds the 30S and 70S subunits. We identify that the key requirement for any EngA-ribosome association is GTP binding to GD2. In this state, EngA displays a weak 50S association, which is further stabilized when GD1 too binds GTP. Exchanging bound GTP with guanosine-5'-diphosphate (GDP), at GD1, results in interactions with 50S, 30S and 70S. Therefore, it appears that GD1 employs GTP hydrolysis as a means to regulate the differential specificity of EngA to either 50S alone or to 50S, 30S and 70S subunits. Furthermore, using constructs lacking either GD1 or both GD1 and GD2, we infer that GD1, when bound to GTP and GDP, adopts distinct conformations to mask or unmask the 30S binding site on EngA. Our results suggest a model where distinct nucleotide-bound states of the two G-domains regulate formation of specific EngA-ribosome complexes.
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