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

Relevance of individual Mo-box nucleotides to DNA binding by the related molybdenum-responsive regulators MopA and MopB in Rhodobacter capsulatus.

FEMS microbiology letters - 1 Jun 2010

Müller Alexandra, Püttmann Lucia, Barthel Romy, Schön Matthias, Lackmann Jan-Wilm, Narberhaus Franz, Masepohl Bernd

Abstract excerpt

Either of two related molybdenum-responsive regulators, MopA and MopB, of Rhodobacter capsulatus is sufficient to repress the nitrogen-fixation gene anfA. In contrast, MopA (but not MopB) activates mop, which codes for a molybdate (Mo)-binding molbindin. Both regulators bind to conserved cis-regu...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Gene Expression Regulation, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Inverted Repeat Sequences

Share to Membrane Transport Proteins

Share to Molybdenum

Share to Plasmids

Share to Promoter Regions, Genetic

Share to Rhodobacter capsulatus

Source

Identifiers

PMID: 20455946
DOI: 10.1111/j.1574-6968.2010.01981.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-20455946-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Relevance of individual Mo-box nucleotides to DNA binding by the related molybdenum-responsive regulators MopA and MopB in Rhodobacter capsulatus.PMID 20455946Read ↗

Promoters controlling expression of the alternative nitrogenase and the molybdenum uptake system in Rhodobacter capsulatus are activated by NtrC, independent of sigma54, and repressed by molybdenum.Semantic proximity Read ↗

Molybdate-dependent expression of dimethylsulfoxide reductase in Rhodobacter capsulatus.Semantic proximity Read ↗

Activity of the molybdopterin-containing xanthine dehydrogenase of Rhodobacter capsulatus can be restored by high molybdenum concentrations in a moeA mutant defective in molybdenum cofactor biosynthesis.Semantic proximity Read ↗

A widespread riboswitch candidate that controls bacterial genes involved in molybdenum cofactor and tungsten cofactor metabolism.Semantic proximity Read ↗

Amino acid residues critical for DNA binding and inducer recognition in CbnR, a LysR-type transcriptional regulator from Cupriavidus necator NH9.Semantic proximity Read ↗

Mutational scanning and affinity cleavage analysis of UhpA-binding sites in the Escherichia coli uhpT promoter.Semantic proximity Read ↗

Role of GlnB and GlnK in ammonium control of both nitrogenase systems in the phototrophic bacterium Rhodobacter capsulatus.Semantic proximity Read ↗

Evidence that regulatory protein MarA of Escherichia coli represses rob by steric hindrance.Semantic proximity Read ↗

Involvement of an unusual mol operon in molybdopterin cofactor biosynthesis in Ralstonia eutropha.Semantic proximity Read ↗

Azorhizobium caulinodans nitrogen fixation (nif/fix) gene regulation: mutagenesis of the nifA -24/-12 promoter element, characterization of a ntrA(rpoN) gene, and derivation of a model.Semantic proximity Read ↗

Mapping and characterization of the promoter elements of the regulatory nif genes rpoN, nifA1 and nifA2 in Rhodobacter capsulatus.Semantic proximity Read ↗

Identification and characterization of the cytoplasmic tungstate/molybdate-binding protein (Mop) from Eubacterium acidaminophilum.Semantic proximity Read ↗

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