Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Expression phenotypes suggest that Der participates in a specific, high affinity interaction with membranes.

Protein expression and purification - 1 Jul 2011

Lee Ryan, Aung-Htut May Thandar, Kwik Charlotte, March Paul E

Abstract excerpt

The GTPase Der is universally conserved in bacteria and is structurally unique as it consists of two GTP-binding domains in tandem (G-domain 1 and G-domain 2) whereas all the other GTPases posses a single GTPase domain. In order to assess the function of Der we have fractionated whole cell lysates containing over expressed Der. This analysis indicated that Der was present in sucrose gradient fractions containing...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacterial Outer Membrane Proteins
Share to Cell Membrane

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Centrifugation, Density Gradient

Share to Escherichia coli Proteins

Share to GTP-Binding Proteins

Share to Guanosine Triphosphate

Share to Recombinant Fusion Proteins

Share to Subcellular Fractions

Source

Identifiers

PMID: 21354313
DOI: 10.1016/j.pep.2011.02.009

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Expression phenotypes suggest that Der participates in a specific, high affinity interaction with membranes.PMID 21354313Read ↗

Heterologous Expression of Der Homologs in an Escherichia coli der Mutant and Their Functional Complementation.Semantic proximity Read ↗

RelA functionally suppresses the growth defect caused by a mutation in the G domain of the essential Der protein.Semantic proximity Read ↗

The widely conserved Era G-protein contains an RNA-binding domain required for Era function in vivo.Semantic proximity Read ↗

Interaction of an essential Escherichia coli GTPase, Der, with the 50S ribosome via the KH-like domain.Semantic proximity Read ↗

DER containing two consecutive GTP-binding domains plays an essential role in chloroplast ribosomal RNA processing and ribosome biogenesis in higher plants.Semantic proximity Read ↗

Crippling the essential GTPase Der causes dependence on ribosomal protein L9.Semantic proximity Read ↗

Deletion of the putative effector region of Era, an essential GTP-binding protein in Escherichia coli, causes a dominant-negative phenotype.Semantic proximity Read ↗

Genetic interaction screens with ordered overexpression and deletion clone sets implicate the Escherichia coli GTPase YjeQ in late ribosome biogenesis.Semantic proximity Read ↗

The GTP binding protein Obg homolog ObgE is involved in ribosome maturation.Semantic proximity Read ↗

Studies of the interaction of Escherichia coli YjeQ with the ribosome in vitro.Semantic proximity Read ↗

Cell cycle arrest in Era GTPase mutants: a potential growth rate-regulated checkpoint in Escherichia coli.Semantic proximity Read ↗

Deficiency of essential GTP-binding protein ObgE in Escherichia coli inhibits chromosome partition.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.