Row-like organization of ATP synthase in intact mitochondria determined by cryo-electron tomography

被引：73

作者：

Dudkina, Natalya V. ^{[1
]}

Oostergetel, Gert T. ^{[1
]}

Lewejohann, Dagmar ^{[2
]}

Braun, Hans-Peter ^{[2
]}

Boekema, Egbert J. ^{[1
]}

机构：

[1] Univ Groningen, Electron Microscopy Grp, Groningen Biomol Sci & Biotechnol Inst, Groningen, Netherlands

[2] Leibniz Univ Hannover, Inst Plant Genet, Fac Nat Sci, Hannover, Germany

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2010年 / 1797卷 / 02期

关键词：

ATP synthase; Electron tomography; Mitochondria; Polytomella; SUPRAMOLECULAR ORGANIZATION; RESOLUTION; CRISTAE; TRANSMISSION; PROTEIN; STALK; DIMER;

D O I：

10.1016/j.bbabio.2009.11.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The fine structure of intact, close-to-spherical mitochondria from the alga Polytomella was visualized by dual-axis cryo-electron tomography. The supramolecular organization of dimeric ATP synthase in the cristae membranes was investigated by averaging subvolumes of tomograms and 3D details at similar to 6 nm resolution were revealed. Oligomeric ATP synthase is composed of rows of dimers at 12 run intervals; the dimers make a slight angle along the row. In addition, the main features of monomeric ATP synthase, such as the conically shaped F, headpiece, central stalk and stator were revealed. This demonstrates the capability of dual-axis electron tomography to unravel details of proteins and their interactions in complete organelles. (C) 2009 Elsevier B.V. All rights reserved.

引用

页码：272 / 277

页数：6

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