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PMID: 8766824 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Transmembrane segment 10 is important for substrate recognition in Ga12 and Hxt2 sugar transporters in the yeast Saccharomyces cerevisiae.

FEBS letters ·Vol. 389 ·No. 2 ·1996-07-01 ·Pages 174-8

Kasahara M, Shimoda E, Maeda M

Abstract

A systematic series of chimeras between Ga12 galactose transporter and Hxt2 glucose transporter in yeast was produced to delineate the essential domain for substrate recognition. A domain of 101 amino acids close to the COOH-terminus that has been previously identified as the critical substrate recognition region was further divided into four subdomains, by introducing five restriction enzyme sites at exactly corresponding locations of both genes without changing coding amino acids. When each of all possible 16 modified genes was expressed, all the galactose transport-active chimeras were found to possess Ga12-derived transmembrane segment (TM) 10. Of the 35 amino acids in the TM1O region, only 12 differ between Ga12 and Hxt2, indicating that these 12 amino acids include the critical residue(s) responsible for the differential recognition of galactose and glucose in these transporters.

MeSH Terms
Amino Acid Sequence Binding Sites Biological Transport Escherichia coli/genetics,metabolism Galactose/metabolism Glucose/metabolism Glucose Transport Proteins, Facilitative Membrane Proteins/chemistry,genetics,metabolism Molecular Sequence Data Monosaccharide Transport Proteins/chemistry,genetics,metabolism Mutation Rec A Recombinases/genetics Recombinant Proteins/chemistry,genetics,metabolism Saccharomyces cerevisiae/chemistry Saccharomyces cerevisiae Proteins Sequence Homology, Amino Acid Substrate Specificity
Chemicals
Glucose Transport Proteins, Facilitative HXT2 protein, S cerevisiae Membrane Proteins Monosaccharide Transport Proteins Recombinant Proteins Saccharomyces cerevisiae Proteins Rec A Recombinases Glucose Galactose
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Kasahara M
Laboratory of Biophysics, School of Medicine, Teikyo University, Hachioji, Tokyo, Japan.
Shimoda E
Maeda M
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1996-07-01
Pages
174-8
Language
English
Region
England
NLM ID
0155157
Subset
IM
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