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

Defective cation-coupling mutants of Escherichia coli Na+/proline symport carrier. Characterization and localization of mutations.

The Journal of biological chemistry - 15 Feb 1990

Yamato I, Ohsawa M, Anraku Y

Abstract excerpt

A major proline carrier in Escherichia coli encoded by the putP gene mediates proline/Na+ or Li+ symport. Proline carrier mutants with altered cation specificity were obtained by mutagenesis with nitrous acid in vitro of a plasmid carrying the wild-type putP gene. Two mutant strains harboring plasmid pMOP4135 and pMOP4141 could transport proline efficiently only in the presence of an increased concentration of...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Base Sequence
Share to Escherichia coli

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

Share to Genes, Bacterial

Share to Genotype

Share to Molecular Sequence Data

Share to Mutation

Share to Plasmids

Source

Identifiers

PMID: 2406235

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

Defective cation-coupling mutants of Escherichia coli Na+/proline symport carrier. Characterization and localization of mutations.PMID 2406235Read ↗

Sodium ion and proline binding sites in the Na+/proline symport carrier of Escherichia coli.Semantic proximity Read ↗

Transmembrane domain II of the Na+/proline transporter PutP of Escherichia coli forms part of a conformationally flexible, cytoplasmic exposed aqueous cavity within the membrane.Semantic proximity Read ↗

Aspartate 55 in the Na+/proline permease of Escherichia coli is essential for Na+-coupled proline uptake.Semantic proximity Read ↗

Proline transport and stress tolerance of ammonia-insensitive mutants of the PUT4-encoded proline-specific permease in yeast.Semantic proximity Read ↗

Ser57 in the Na+/proline permease of Escherichia coli is critical for high-affinity proline uptake.Semantic proximity Read ↗

Identification and characterization of functional residues in a Na+/H+ antiporter (NhaA) from Escherichia coli by random mutagenesis.Semantic proximity Read ↗

Proline dehydrogenase activity of the transcriptional repressor PutA is required for induction of the put operon by proline.Semantic proximity Read ↗

The transmembrane domains of the sensor kinase KdpD of Escherichia coli are not essential for sensing K+ limitation.Semantic proximity Read ↗

Evidence for a sodium-dependent proline and glycine-betaine uptake in the cyanobacterium Nostoc muscorum.Semantic proximity Read ↗

Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase.Semantic proximity Read ↗

Low-proline environments impair growth, proline transport and in vivo survival of Staphylococcus aureus strain-specific putP mutants.Semantic proximity Read ↗

Characterization of Escherichia coli glnL mutations affecting nitrogen regulation.Semantic proximity Read ↗

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