NDLI: Obstruction of Transmembrane Helical Movements in Subunit a Blocks Proton Pumping by $F_{1}F_{o}$ ATP Synthase

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Obstruction of Transmembrane Helical Movements in Subunit a Blocks Proton Pumping by $F_{1}F_{o}$ ATP Synthase

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Obstruction of Transmembrane Helical Movements in Subunit a Blocks Proton Pumping by $F_{1}F_{o}$ ATP Synthase

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Moore, Kyle J. Fillingame, Robert H.
Description	Author Affiliation: Moore KJ ( Department of Biomolecular Chemistry, School of Medicine, and Public Health, University of Wisconsin, Madison, Wisconsin 53706, USA.)
Abstract	Subunit a plays a key role in promoting H(+) transport-coupled rotary motion of the subunit c ring in F1Fo ATP synthase. H(+) binding and release occur at Asp-61 in the middle of the second transmembrane helix (TMH) of Fo subunit c. H(+) are thought to reach cAsp61 via aqueous half-channels formed by TMHs 2-5 of subunit a. Movements of TMH4 and TMH5 have been proposed to facilitate protonation of cAsp61 from a half channel centered in a four helix bundle at the periplasmic side of subunit a. The possible necessity of these proposed TMH movements was investigated by assaying ATP driven H(+) pumping function before and after cross-linking paired Cys substitutions at the center of TMHs within subunit a. The cross-linking of the Cys pairs aG218C/I248C in TMH4 and TMH5, and aL120C/H245C in TMH2 and TMH5, inhibited H(+) pumping by 85-90%. H(+) pumping function was largely unaffected by modification of the same Cys residues in the absence of cross-link formation. The inhibition is consistent with the proposed requirement for TMH movements during the gating of periplasmic H(+) access to cAsp61. The cytoplasmic loops of subunit a have been implicated in gating H(+) release to the cytoplasm, and previous cross-linking experiments suggest that the chemically reactive regions of the loops may pack as a single domain. Here we show that Cys substitutions in these domains can be cross-linked with retention of function and conclude that these domains need not undergo large conformational changes during enzyme function.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	35
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-08-30
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proton-Translocating ATPases Chemistry Escherichia Coli Proteins Escherichia Coli Enzymology Amino Acid Substitution Genetics Metabolism Mutation, Missense Protein Structure, Secondary Protein Structure, Tertiary Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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