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

Effects of streptomycin resistance mutations on posttranslational modification of ribosomal protein S12.

Journal of bacteriology - 1 Mar 2006

Carr Jennifer F, Hamburg Daisy-Malloy, Gregory Steven T, Limbach Patrick A, Dahlberg Albert E

Abstract excerpt

Ribosomal protein S12 contains a highly conserved aspartic acid residue that is posttranslationally beta-methylthiolated. Using mass spectrometry, we have determined the modification states of several S12 mutants of Thermus thermophilus and conclude that beta-methylthiolation is not a determinant of the streptomycin phenotype.

Read the complete abstract on PubMed

Topics

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

Share to Aspartic Acid
Share to Bacillus subtilis
Share to Drug Resistance, Bacterial

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

Share to Protein Processing, Post-Translational

Share to Ribosomal Proteins

Share to Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Share to Streptomycin

Share to Thermus thermophilus

Source

Open in PubMed Open full text

Identifiers

PMID: 16484214
DOI: 10.1128/JB.188.5.2020-2023.2006
PMCID: PMC1426572

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effects of streptomycin resistance mutations on posttranslational modification of ribosomal protein S12.PMID 16484214Read ↗

Severity of the streptomycin resistance and streptomycin dependence phenotypes of ribosomal protein S12 of Thermus thermophilus depends on the identity of highly conserved amino acid residues.Semantic proximity Read ↗

A proteomic and transcriptomic approach reveals new insight into beta-methylthiolation of Escherichia coli ribosomal protein S12.Semantic proximity Read ↗

Thermus thermophilus L11 methyltransferase, PrmA, is dispensable for growth and preferentially modifies free ribosomal protein L11 prior to ribosome assembly.Semantic proximity Read ↗

Error-prone and error-restrictive mutations affecting ribosomal protein S12.Semantic proximity Read ↗

Diverse effects of residues 74-78 in ribosomal protein S12 on decoding and antibiotic sensitivity.Semantic proximity Read ↗

Structural and functional studies of the Thermus thermophilus 16S rRNA methyltransferase RsmG.Semantic proximity Read ↗

Streptomycin-resistant and streptomycin-dependent mutants of the extreme thermophile Thermus thermophilus.Semantic proximity Read ↗

Isolation and characterization of Bacillus stearothermophilus 30S and 50S ribosomal protein mutations.Semantic proximity Read ↗

Mutational analysis of 16S and 23S rRNA genes of Thermus thermophilus.Semantic proximity Read ↗

Thiostrepton-resistant mutants of Thermus thermophilus.Semantic proximity Read ↗

Single ribosomal protein mutations in antibiotic-resistant bacteria analyzed by mass spectrometry.Semantic proximity Read ↗

Solution structures and backbone dynamics of the ribosomal protein S6 and its permutant P(54-55).Semantic proximity Read ↗

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