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

Mapping RNA-protein interactions in ribonuclease P from Escherichia coli using disulfide-linked EDTA-Fe.

Journal of molecular biology - 11 Feb 2000

Biswas R, Ledman D W, Fox R O, Altman S, Gopalan V

Abstract excerpt

The protein subunit of Escherichia coli ribonuclease P (which has a cysteine residue at position 113) and its single cysteine-substituted mutant derivatives (S16C/C113S, K54C/C113S and K66C/C113S) have been modified using a sulfhydryl-specific iron complex of EDTA-2- aminoethyl 2-pyridyl disulfide (EPD-Fe). This reaction converts C5 protein, or its single cysteine-substituted mutant derivatives, into chemical...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Disulfides
Share to Edetic Acid

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Endoribonucleases

Share to Holoenzymes

Share to Hydroxyl Radical

Share to Ribonuclease P

Share to RNA, Catalytic

Source

Identifiers

PMID: 10656815
DOI: 10.1006/jmbi.1999.3443

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Mapping RNA-protein interactions in ribonuclease P from Escherichia coli using disulfide-linked EDTA-Fe.PMID 10656815Read ↗

Mapping protein-protein interactions by localized oxidation: consequences of the reach of hydroxyl radical.Semantic proximity Read ↗

Defining the enzyme binding domain of a ribonuclease III processing signal. Ethylation interference and hydroxyl radical footprinting using catalytically inactive RNase III mutants.Semantic proximity Read ↗

A Pro to His mutation in active site of thioredoxin increases its disulfide-isomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonuclease.Semantic proximity Read ↗

Folding and unfolding kinetics of the proline-to-alanine mutants of bovine pancreatic ribonuclease A.Semantic proximity Read ↗

The RNR motif of B. subtilis RNase P protein interacts with both PRNA and pre-tRNA to stabilize an active conformer.Semantic proximity Read ↗

Conformationally Dynamic Radical Transfer within Ribonucleotide Reductase.Semantic proximity Read ↗

Bacterial ribonuclease P holoenzyme crosslinking analysis reveals protein interaction sites on the RNA subunit.Semantic proximity Read ↗

Characterization of C439SR1, a mutant of Escherichia coli ribonucleotide diphosphate reductase: evidence that C439 is a residue essential for nucleotide reduction and C439SR1 is a protein possessing novel thioredoxin-like activity.Semantic proximity Read ↗

Lead-catalyzed cleavage of ribonuclease P RNA as a probe for integrity of tertiary structure.Semantic proximity Read ↗

Structure of an archaeal homolog of the human protein complex Rpp21-Rpp29 that is a key core component for the assembly of active ribonuclease P.Semantic proximity Read ↗

Interaction of C225SR1 mutant subunit of ribonucleotide reductase with R2 and nucleoside diphosphates: tales of a suicidal enzyme.Semantic proximity Read ↗

Protein component of the ribozyme ribonuclease P alters substrate recognition by directly contacting precursor tRNA.Semantic proximity Read ↗

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