ArticleThe Journal of biological chemistry2010
Identification of a key residue determining substrate affinity in the yeast glucose transporter Hxt7: a two-dimensional comprehensive study.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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.
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.
Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- Key amino acid residues govern the substrate selectivity of the transporter Xltr1p fromEngineering microbiology · 2024Article
- Specialization Restricts the Evolutionary Paths Available to Yeast Sugar Transporters.Molecular biology and evolution · 2024Article
- Specialization restricts the evolutionary paths available to yeast sugar transporters.bioRxiv : the preprint server for biology · 2024Article
- Establishing mammalian GLUT kinetics and lipid composition influences in a reconstituted-liposome system.Nature communications · 2023Article
- Strategies for Efficient Expression of Heterologous Monosaccharide Transporters inJournal of fungi (Basel, Switzerland) · 2022Article
- Identification of key residues for efficient glucose transport by the hexose transporter CgHxt4 in high sugar fermentation yeast Candida glycerinogenes.Applied microbiology and biotechnology · 2021Article
- Structures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS).Chemical reviews · 2021Article
- Low affinity uniporter carrier proteins can increase net substrate uptake rate by reducing efflux.Scientific reports · 2018Article
- Xylose Fermentation by Saccharomyces cerevisiae: Challenges and Prospects.International journal of molecular sciences · 2016Review
- Engineering of yeast hexose transporters to transport D-xylose without inhibition by D-glucose.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Rewiring yeast sugar transporter preference through modifying a conserved protein motif.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Single amino acid substitutions in HXT2.4 from Scheffersomyces stipitis lead to improved cellobiose fermentation by engineered Saccharomyces cerevisiae.Applied and environmental microbiology · 2013Article
- Delineating the extracellular water-accessible surface of the proton-coupled folate transporter.PloS one · 2013Article
- How yeast re-programmes its transcriptional profile in response to different nutrient impulses.BMC systems biology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We previously identified Asn(331) in transmembrane segment 7 (TM7) as a key residue determining substrate affinity in Hxt2, a moderately high-affinity facilitative glucose transporter of Saccharomyces cerevisiae. To gain further insight into the structural basis of substrate recognition by yeast glucose transporters, we have now studied Hxt7, whose affinity for glucose is the highest among the major hexose transporters. The functional role of Asp(340) in Hxt7, the residue corresponding to Asn(331) of Hxt2, was examined by replacing it with each of the other 19 amino acids. Such replacement of Asp(340) generated transporters with various affinities for glucose, with the affinity of the Cys(340) mutant surpassing that of the wild-type Hxt7. To examine the structural role of Asp(340) in the substrate translocation pathway, we performed cysteine-scanning mutagenesis of the 21 residues in TM7 of a functional Cys-less Hxt7 mutant in conjunction with exposure to the hydrophilic sulfhydryl reagent p-chloromercuribenzenesulfonate (pCMBS). The transport activity of the D340C mutant of Cys-less Hxt7, in which Asp(340) is replaced with Cys, was completely inhibited by pCMBS, indicating that Asp(340) is located in a water-accessible position. This D340C mutant showed a sensitivity to pCMBS that was approximately 70 times that of the wild-type Hxt7, and it was protected from pCMBS inhibition by the substrates d-glucose and 2-deoxy-d-glucose but not by l-glucose. These results indicate that Asp(340) is situated at or close to a substrate recognition site and is a key residue determining high-affinity glucose transport by Hxt7, supporting the notion that yeast glucose transporters share a common mechanism for substrate recognition.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.