Journal article
Interactions between subunits a and b in the rotary ATP synthase as determined by cross-linking
- Abstract:
- The interaction of the membrane traversing stator subunits a and b of the rotary ATP synthase was probed by substitution of a single Cys into each subunit with subsequent Cu2+ catalyzed cross-linking. Extensive interaction between the transmembrane (TM) region of one b subunit and TM2 of subunit a was indicated by cross-linking with 6 Cys pairs introduced into these regions. Additional disulfide cross-linking was observed between the N-terminus of subunit b and the periplasmic loop connecting TM4 and TM5 of subunit a. Finally, benzophenone-4-maleimide derivatized Cys in the 2–3 periplasmic loop of subunit a were shown to cross-link with the periplasmic N-terminal region of subunit b. These experiments help to define the juxtaposition of subunits b and a in the ATP synthase.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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- Files:
-
-
(Preview, Accepted manuscript, pdf, 3.7MB, Terms of use)
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- Publisher copy:
- 10.1016/j.febslet.2013.02.012
Authors
- Publisher:
- Elsevier
- Journal:
- FEBS Letters More from this journal
- Volume:
- 587
- Issue:
- 7
- Pages:
- 892-897
- Publication date:
- 2013-02-14
- Acceptance date:
- 2013-02-14
- DOI:
- EISSN:
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1873-3468
- ISSN:
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0014-5793
- Pmid:
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23416299
- Language:
-
English
- Keywords:
- Pubs id:
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389271
- Local pid:
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pubs:389271
- Deposit date:
-
2023-07-28
Terms of use
- Copyright holder:
- Federation of European Biochemical Societies
- Copyright date:
- 2013
- Rights statement:
- © 2013 Federation of European Biochemical Societies
- Notes:
- This is the accepted manuscript version of the article. The final version is available online from Elsevier at https://dx.doi.org/10.1016/j.febslet.2013.02.012
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