Discover Community Create You

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

Membrane association via an amino-terminal amphipathic helix is required for the cellular organization and function of RNase II.

The Journal of biological chemistry - 8 Mar 2013

Lu Feng, Taghbalout Aziz

Abstract excerpt

The subcellular localization of the exoribonuclease RNase II is not known despite the advanced biochemical characterization of the enzyme. Here we report that RNase II is organized into cellular structures that appear to coil around the Escherichia coli cell periphery and that RNase II is associated with the cytoplasmic membrane by its amino-terminal amphipathic helix. The helix also acts as an autonomous...

Read the complete abstract on PubMed

Topics

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

Share to Cell Membrane
Share to Escherichia coli Proteins
Share to Exoribonucleases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrophobic and Hydrophilic Interactions

Share to Luminescent Proteins

Share to Microbial Viability

Share to Microscopy, Fluorescence

Share to Protein Structure, Secondary

Source

Open in PubMed Open full text

Identifiers

PMID: 23344958
DOI: 10.1074/jbc.M112.408674
PMCID: PMC3591632

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Membrane association via an amino-terminal amphipathic helix is required for the cellular organization and function of RNase II.PMID 23344958Read ↗

The RNase E of Escherichia coli is a membrane-binding protein.Semantic proximity Read ↗

Mechanistic insights on the folding of a large ribozyme during transcription.Semantic proximity Read ↗

RNaseE and RNA helicase B play central roles in the cytoskeletal organization of the RNA degradosome.Semantic proximity Read ↗

Identification and characterization of a new lipoprotein, NlpI, in Escherichia coli K-12.Semantic proximity Read ↗

RNase activity of polynucleotide phosphorylase is critical at low temperature in Escherichia coli and is complemented by RNase II.Semantic proximity Read ↗

RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton.Semantic proximity Read ↗

Cooperative transitions of isolated Escherichia coli nucleoids: implications for the nucleoid as a cellular phase.Semantic proximity Read ↗

Type A and B RNase P RNAs are interchangeable in vivo despite substantial biophysical differences.Semantic proximity Read ↗

RNase II regulates RNase PH and is essential for cell survival during starvation and stationary phase.Semantic proximity Read ↗

Oligoribonuclease is an essential component of the mRNA decay pathway.Semantic proximity Read ↗

Buried hydrophobic side-chains essential for the folding of the parallel beta-helix domains of the P22 tailspike.Semantic proximity Read ↗

Membrane assembly of circularly permuted variants of the E. coli outer membrane protein OmpA.Semantic proximity Read ↗

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