Details
| Original language | English |
|---|---|
| Pages (from-to) | 3427-3432 |
| Number of pages | 6 |
| Journal | FEBS letters |
| Volume | 580 |
| Issue number | 14 |
| Publication status | Published - 12 May 2006 |
Abstract
There is increasing evidence now that F1F0 ATP synthase is arranged in dimers in the inner mitochondrial membrane of several organisms. The dimers are also considered to be the building blocks of oligomers. It was recently found that the monomers in beef and the alga Polytomella ATP synthase dimer make an angle of ∼40° and ∼70°, respectively. This arrangement is considered to induce a strong local bending of the membrane. To further understand the packing of dimers into oligomers we performed an electron microscopy analysis of ATP synthase dimers purified from Saccharomyces cerevisiae. Two types of dimers were found in which the angle between the monomers is either ∼90° or ∼35°. According to our interpretation, the wide-angle dimers (70-90°) are "true-dimers" whereas the small-angle dimers (35-40°) rather are "pseudo-dimers", which represent breakdown products of two adjacent true dimers in the oligomer. Ultrathin sectioning of intact Polytomella mitochondria indicates that the inner mitochondrial or cristae membrane is folded into lamellae and tubuli. Oligomers of ATP synthase can arrange in a helical fashion in tubular-shaped cristae membranes. These results strongly support the hypothesized role of ATP synthase oligomers in structural determination of the mitochondrial inner membrane.
Keywords
- ATP synthase, Dimer, Electron microscopy, Mitochondria, Polytomella, Saccharomyces cerevisiae
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biophysics
- Biochemistry, Genetics and Molecular Biology(all)
- Structural Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
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In: FEBS letters, Vol. 580, No. 14, 12.05.2006, p. 3427-3432.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Characterization of dimeric ATP synthase and cristae membrane ultrastructure from Saccharomyces and Polytomella mitochondria
AU - Dudkina, Natalya V.
AU - Sunderhaus, Stephanie
AU - Braun, Hans Peter
AU - Boekema, Egbert J.
N1 - Funding information: We thank Mr. Ruby Kalicharan for expert technical assistance. H.P.B. acknowledges a grant of the Deutsche Forschungsgemeinschaft (Br1829-7/1) and E.J.B. grants of the Dutch science foundation NWO-CW.
PY - 2006/5/12
Y1 - 2006/5/12
N2 - There is increasing evidence now that F1F0 ATP synthase is arranged in dimers in the inner mitochondrial membrane of several organisms. The dimers are also considered to be the building blocks of oligomers. It was recently found that the monomers in beef and the alga Polytomella ATP synthase dimer make an angle of ∼40° and ∼70°, respectively. This arrangement is considered to induce a strong local bending of the membrane. To further understand the packing of dimers into oligomers we performed an electron microscopy analysis of ATP synthase dimers purified from Saccharomyces cerevisiae. Two types of dimers were found in which the angle between the monomers is either ∼90° or ∼35°. According to our interpretation, the wide-angle dimers (70-90°) are "true-dimers" whereas the small-angle dimers (35-40°) rather are "pseudo-dimers", which represent breakdown products of two adjacent true dimers in the oligomer. Ultrathin sectioning of intact Polytomella mitochondria indicates that the inner mitochondrial or cristae membrane is folded into lamellae and tubuli. Oligomers of ATP synthase can arrange in a helical fashion in tubular-shaped cristae membranes. These results strongly support the hypothesized role of ATP synthase oligomers in structural determination of the mitochondrial inner membrane.
AB - There is increasing evidence now that F1F0 ATP synthase is arranged in dimers in the inner mitochondrial membrane of several organisms. The dimers are also considered to be the building blocks of oligomers. It was recently found that the monomers in beef and the alga Polytomella ATP synthase dimer make an angle of ∼40° and ∼70°, respectively. This arrangement is considered to induce a strong local bending of the membrane. To further understand the packing of dimers into oligomers we performed an electron microscopy analysis of ATP synthase dimers purified from Saccharomyces cerevisiae. Two types of dimers were found in which the angle between the monomers is either ∼90° or ∼35°. According to our interpretation, the wide-angle dimers (70-90°) are "true-dimers" whereas the small-angle dimers (35-40°) rather are "pseudo-dimers", which represent breakdown products of two adjacent true dimers in the oligomer. Ultrathin sectioning of intact Polytomella mitochondria indicates that the inner mitochondrial or cristae membrane is folded into lamellae and tubuli. Oligomers of ATP synthase can arrange in a helical fashion in tubular-shaped cristae membranes. These results strongly support the hypothesized role of ATP synthase oligomers in structural determination of the mitochondrial inner membrane.
KW - ATP synthase
KW - Dimer
KW - Electron microscopy
KW - Mitochondria
KW - Polytomella
KW - Saccharomyces cerevisiae
UR - http://www.scopus.com/inward/record.url?scp=33646934708&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2006.04.097
DO - 10.1016/j.febslet.2006.04.097
M3 - Article
C2 - 16714019
AN - SCOPUS:33646934708
VL - 580
SP - 3427
EP - 3432
JO - FEBS letters
JF - FEBS letters
SN - 0014-5793
IS - 14
ER -