NDLI: Identification of conserved polar residues important for salt tolerance by the Na$^{+}$/H$^{+}$ exchanger of Schizosaccharomyces pombe

Content Provider	Springer Nature Link
Author	Fliegel, Larry
Copyright Year	2005
Abstract	The Na$^{+}$/H$^{+}$ exchanger is a ubiquitous protein that transports Na$^{+}$ and H$^{+}$ in opposite directions across cell membranes. In fission yeast, the Na$^{+}$/H$^{+}$ exchanger sod2 plays a major role in the removal of excess detrimental intracellular sodium. The effect of mutagenesis of conserved polar amino acids of sod2 was examined by expressing 10 different mutant forms of sod2 in sod2 deficient S. pombe and characterizing salt tolerance. Asp145, 266, 267, and Glu173 were critical for proper function of sod2. Asp241 had an intermediate effect on sod2 function while mutation of Asp178 did not impair sod2 function. Simultaneous mutation of the Asp266, 267 pair impaired sod2 function. Mutation of each individual residue demonstrated that both were critical for sod2 function. Conservative mutations (Asp to Glu) of Asp266 and 267 failed to restore sod2 function. The results suggest that acidic residues associated with transmembrane segments are important in function, possibly being important in binding and coordinating cations. (Mol Cell Biochem 268: 83–92, 2005)
Starting Page	83
Ending Page	92
Page Count	10
File Format	PDF
ISSN	03008177
Journal	Molecular and Cellular Biochemistry
Volume Number	268
Issue Number	1-2
e-ISSN	15734919
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2005-01-01
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Na$^{+}$/H$^{+}$ exchanger Schizosaccharomyces pombe, cation binding salt tolerance Cardiology Medical Biochemistry Oncology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine Clinical Biochemistry Molecular Biology

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