Effect of point substitutions of Asp-714 and Asp-720 residues on the structure and function of the H+-ATPase of the yeast ... View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2014-09

AUTHORS

V. V. Petrov, R. I. Ibragimov

ABSTRACT

Membrane-spanning M5 and M6 segments, which play a role in the formation of cation transport sites in H+-, Ca2+-, K+-, Na+-, and other P2-ATPases, are connected by a short extracytoplasmic loop. In the yeast plasma membrane H+-ATPase, which belongs to a family of P2-ATPases, the loop is connected to M5 and M6 through the Asp-714 and Asp-720 residues. In this work, the effect of point amino acid replacements of Asp-714 and Asp-720 by Ala, Val, Asn, and Glu residues on the function of the enzyme was studied. The D714A point mutant possessed activities similar to those of the wild-type enzyme, whereas the replacement of Asp-714 by other amino acid residues disrupted biogenesis and led to a loss of activity. All mutants with substitution of Asp-720 were expressed and possessed relatively high activity. The D720V mutant displayed significantly reduced expression level, activity, H+ transport and its coupling to ATP hydrolysis. Thus, substitutions of Asp-714, except for the D714N mutant, led to significant defects in biogenesis and/or function of the enzyme. The results indicate the important role for the Asp-714 residue in biogenesis, structure stability, and enzyme function. More... »

PAGES

508-515

Identifiers

URI

http://scigraph.springernature.com/pub.10.1134/s000368381405007x

DOI

http://dx.doi.org/10.1134/s000368381405007x

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1011016530


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