Evidence map›Paper›PMID 8955402›Full record

ArticleJournal of bacteriology1996

Amino acid substitutions in membrane-spanning domains of Hol1, a member of the major facilitator superfamily of transporters, confer nonselective cation uptake in Saccharomyces cerevisiae.

M B Wright, E A Howell, R F Gaber

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.8field-weighted citation impact, top 27% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The mycoparasitic fungusEvolutionary applications · 2018
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Phenotypic effects of membrane protein overexpression in Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  11. Article
  12. Article
  13. Posttranscriptional control of gene expression in yeast.Microbiology and molecular biology reviews : MMBR · 1998
    Review
  14. Article
  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

M B WrightDepartment of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA.
E A Howell
R F Gaber
Northwestern University · US

Funding

TRANSCRIPTIONAL MODULATION IN YEASTR01GM045739 · NIGMS · NORTHWESTERN UNIVERSITY · PI GABER, RICHARD F · 1991 to 1994
–
NIGMS NIH HHS GM45739
6 · The paper itself

Abstract

Selection for the ability of Saccharomyces cerevisiae cells to take up histidinol, the biosynthetic precursor to histidine, results in dominant mutations at HOL1. The DNA sequence of HOL1 was determined, and it predicts a 65-kDa protein related to the major facilitator family (drug resistance subfamily) of putative transport proteins. Two classes of mutations were obtained: (i) those that altered the coding region of HOL1, conferring the ability to take up histidinol; and (ii) cis-acting mutations (selected in a mutant HOL1-1 background) that increased expression of the Hol1 protein. The ability to transport histidinol and other cations was conferred by single amino acid substitutions at any of three sites located within putative membrane-spanning domains of the transporter. These mutations resulted in the conversion of a small hydrophobic amino acid codon to a phenylalanine codon. Selection for spontaneous mutations that increase histidinol uptake by such HOL1 mutants resulted in mutations that abolish the putative start codon of a six-codon open reading frame located approximately 171 nucleotides downstream of the transcription initiation site and 213 nucleotides upstream of the coding region of HOL1. This single small upstream open reading frame (uORF) confers translational repression upon HOL1; genetic disruption of the putative start codon of the uORF results in a 5- to 10-fold increase in steady-state amounts of Hol1 protein without significantly affecting the level of HOL1 mRNA expression.

Indexed as

AllelesAmino Acid SequenceBase SequenceBinding SitesCarrier ProteinsCations, DivalentDNA, FungalGene DeletionHistidinolMembrane ProteinsMolecular Sequence DataOpen Reading FramesPotassiumProtein BiosynthesisSaccharomyces cerevisiaeSequence Homology, Amino AcidCarrier ProteinsCations, DivalentDNA, FungalHistidinolMembrane ProteinsPotassium

Identifiers

PMID8955402
PMCPMC178633
OpenAlexW2157611510

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.