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

The purine-cytosine permease gene of Saccharomyces cerevisiae: primary structure and deduced protein sequence of the FCY2 gene product.

Molecular microbiology - 1 Apr 1990

Weber E, Rodriguez C, Chevallier M R, Jund R

Abstract excerpt

A 2.1 kb DNA segment carrying the purine-cytosine permease gene (FCY2) of Saccharomyces cerevisiae was sequenced, the primary structure of the protein (533 amino acids) deduced and a folding pattern in the membrane is proposed for the permease protein. Expression of the FCY2 gene product requires a functional secretory pathway and is reduced in mnn9, a mutant strain deficient in outer chain glycosylation. The...

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 Genes, Fungal

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

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Conformation

Share to Restriction Mapping

Share to Saccharomyces cerevisiae

Source

Identifiers

PMID: 2191181
DOI: 10.1111/j.1365-2958.1990.tb00627.x

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

The purine-cytosine permease gene of Saccharomyces cerevisiae: primary structure and deduced protein sequence of the FCY2 gene product.PMID 2191181Read ↗

New plasmid system to select for Saccharomyces cerevisiae purine-cytosine permease affinity mutants.Semantic proximity Read ↗

Screening of an intragenic second-site suppressor of purine-cytosine permease from Saccharomyces cerevisiae. Possible role of Ser272 in the base translocation process.Semantic proximity Read ↗

Replacement of Lys by Glu in a transmembrane segment strongly impairs the function of the uracil permease from Saccharomyces cerevisiae.Semantic proximity Read ↗

In vivo and in vitro studies of the purine-cytosine permease of Saccharomyces cerevisiae. Functional analysis of a mutant with an altered apparent transport constant of uptake.Semantic proximity Read ↗

Folding proteome of Yarrowia lipolytica targeting with uracil permease mutants.Semantic proximity Read ↗

Evidence for a dynamic role for proline376 in the purine-cytosine permease of Saccharomyces cerevisiae.Semantic proximity Read ↗

Functional analyses of yeast purine-cytosine permease mutants.Semantic proximity Read ↗

Mutational analysis of functional domains in Mrs2p, the mitochondrial Mg2+ channel protein of Saccharomyces cerevisiae.Semantic proximity Read ↗

Carboxypeptidase yscS: gene structure and function of the vacuolar enzyme.Semantic proximity Read ↗

Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids.Semantic proximity Read ↗

Sequence and function analysis of a 4.3 kb fragment of Saccharomyces cerevisiae chromosome II including three open reading frames.Semantic proximity Read ↗

The study of methionine uptake in Saccharomyces cerevisiae reveals a new family of amino acid permeases.Semantic proximity Read ↗

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