Transmembrane Segment XI of the Na+/H+ Antiporter of S. pombe is a Critical Part of the Ion Translocation Pore. Sci Rep 2017 Oct 16;7(1):12793
Date
10/19/2017Pubmed ID
29038548Pubmed Central ID
PMC5643542DOI
10.1038/s41598-017-12701-zScopus ID
2-s2.0-85031748185 (requires institutional sign-in at Scopus site) 4 CitationsAbstract
The Na+/H+ exchanger of the plasma membrane of S. pombe (SpNHE1) removes intracellular sodium in exchange for an extracellular proton. We examined the structure and functional role of amino acids 360-393 of putative transmembrane (TM) segment XI of SpNHE1. Structural analysis suggested that it had a helical propensity over amino acids 360-368, an extended region from 369-378 and was helical over amino acids 379-386. TM XI was sensitive to side chain alterations. Mutation of eight amino acids to alanine resulted in loss of one or both of LiCl or NaCl tolerance when re-introduced into SpNHE1 deficient S. pombe. Mutation of seven other amino acids had minor effects. Analysis of structure and functional mutations suggested that Glu361 may be involved in cation coordination on the cytoplasmic face of the protein with a negative charge in this position being important. His367, Ile371 and Gly372 were important in function. Ile371 may have important hydrophobic interactions with other residues and Gly372 may be important in maintaining an extended conformation. Several residues from Val377 to Leu384 are important in function possibly involved in hydrophobic interactions with other amino acids. We suggest that TM XI forms part of the ion translocation core of this Na+/H+ exchanger.
Author List
Dutta D, Shin K, Rainey JK, Fliegel LAuthor
Kyungsoo Shin PhD Assistant Professor in the Biophysics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceBiological Transport
Cell Membrane
Gene Expression Regulation, Fungal
Ions
Magnetic Resonance Spectroscopy
Models, Molecular
Mutagenesis
Schizosaccharomyces
Schizosaccharomyces pombe Proteins
Sodium-Hydrogen Exchangers