Solution structure of subunit a, a₁₀₄₋₃₆₃, of the Saccharomyces cerevisiae V-ATPase and the importance of its C-terminus in structure formation.

Journal of Bioenergetics and Biomembranes
Phat Vinh DipGerhard Grüber

Abstract

The 95 kDa subunit a of eukaryotic V-ATPases consists of a C-terminal, ion-translocating part and an N-terminal cytosolic domain. The latter's N-terminal domain (~40 kDa) is described to bind in an acidification-dependent manner with cytohesin-2 (ARNO), giving the V-ATPase the putative function as pH-sensing receptor. Recently, the solution structure of the very N-terminal segment of the cytosolic N-terminal domain has been solved. Here we produced the N-terminal truncated form SCa₁₀₄₋₃₆₃ of the N-terminal domain (SCa₁₋₃₆₃) of the Saccharomyces cerevisiae V-ATPase and determined its low resolution solution structure, derived from SAXS data. SCa₁₀₄₋₃₆₃ shows an extended S-like conformation with a width of about 3.88 nm and a length of 11.4 nm. The structure has been superimposed into the 3D reconstruction of the related A₁A₀ ATP synthase from Pyrococcus furiosus, revealing that the SCa₁₀₄₋₃₆₃ fits well into the density of the collar structure of the enzyme complex. To understand the importance of the C-terminus of the protein SCa₁₋₃₆₃, and to determine the localization of the N- and C-termini in SCa₁₀₄₋₃₆₃, the C-terminal truncated form SCa₁₀₆₋₃₂₄ was produced and analyzed by SAXS. Comparison of the SCa₁₀₄₋₃₆₃ and SCa₁₀₆₋₃₂₄ sha...Continue Reading

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Citations

Jan 5, 2013·The Journal of Biological Chemistry·Hiroyuki HosokawaVladimir Marshansky
Feb 11, 2014·Biochimica Et Biophysica Acta·Vladimir MarshanskyGerhard Grüber
Apr 8, 2015·The Journal of Physical Chemistry. B·Po-Min ShihShang-Te Danny Hsu

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