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

Robust translation of the nucleoid protein Fis requires a remote upstream AU element and is enhanced by RNA secondary structure.

Journal of bacteriology - 1 May 2012

Nafissi Maryam, Chau Jeannette, Xu Jimin, Johnson Reid C

Abstract excerpt

Synthesis of the Fis nucleoid protein rapidly increases in response to nutrient upshifts, and Fis is one of the most abundant DNA binding proteins in Escherichia coli under nutrient-rich growth conditions. Previous work has shown that control of Fis synthesis occurs at transcription initiation of the dusB-fis operon. We show here that while translation of the dihydrouridine synthase gene dusB is low, unusual...

Read the complete abstract on PubMed

Topics

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

Share to Escherichia coli
Share to Escherichia coli Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Expression Regulation, Bacterial

Share to Nucleic Acid Conformation

Share to Operon

Share to Protein Biosynthesis

Share to Reverse Transcriptase Polymerase Chain Reaction

Share to RNA, Bacterial

Source

Open in PubMed Open full text

Identifiers

PMID: 22389479
DOI: 10.1128/JB.00053-12
PMCID: PMC3347164

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Robust translation of the nucleoid protein Fis requires a remote upstream AU element and is enhanced by RNA secondary structure.PMID 22389479Read ↗

RluA is the major mRNA pseudouridine synthase in <i>Escherichia coli</i>Semantic proximity Read ↗

TusA Is a Versatile Protein That Links Translation Efficiency to Cell Division in Escherichia coli.Semantic proximity Read ↗

RNA secondary structure regulates the translation of sxy and competence development in Haemophilus influenzae.Semantic proximity Read ↗

The ancestral SgrS RNA discriminates horizontally acquired Salmonella mRNAs through a single G-U wobble pair.Semantic proximity Read ↗

Discovery of Pyrobaculum small RNA families with atypical pseudouridine guide RNA features.Semantic proximity Read ↗

An Alternative Role of RluD in the Fidelity of Translation Initiation in Escherichia coli.Semantic proximity Read ↗

Comparative study of two box H/ACA ribonucleoprotein pseudouridine-synthases: relation between conformational dynamics of the guide RNA, enzyme assembly and activity.Semantic proximity Read ↗

Pseudouridine-Free Escherichia coli Ribosomes.Semantic proximity Read ↗

AU-rich sequences within 5' untranslated leaders enhance translation and stabilize mRNA in Escherichia coli.Semantic proximity Read ↗

Unraveling the RNA Binding Properties of the Iron-Sulfur Zinc Finger Protein CPSF30.Semantic proximity Read ↗

The Bacillus subtilis iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteins.Semantic proximity Read ↗

Haloferax volcanii, a prokaryotic species that does not use the Shine Dalgarno mechanism for translation initiation at 5'-UTRs.Semantic proximity Read ↗

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