Localization and Organization of the Translational Apparatus in Mitochondrial Membranes of Astasia longa

Localization and Organization of the Translational Apparatus in Mitochondrial Membranes of... In isolated mitochondrial membranes of Astasia longa, large and small circular substructures were observed with diameters of 1.30 and 0.35 μm and thickness of 0.08 and 0.03 μm, respectively. Such substructures were isolated by membrane treatment with proteolytic enzymes (proteinase K, trypsin) or by lipid solubilization with Triton X-100. After the removal of surface protein layer, we uncovered circular polyribosomes with similar diameters as those of original substructures. Polyribosomes were identified on the basis of their morphology, positive staining with uranyl acetate, a capacity for chloramphenicol-sensitive incorporation of 14C-amino acids into polypeptides, and from their buoyant density as estimated by equilibrium centrifugation in the CsCl density gradient. The conclusion is that, in mitochondrial membranes of A. longa, the translational apparatus is organized similarly to that in the membranes of chloroplasts and cyanobacteria, e.g., large and small circular polyribosomes situated within the membrane ring-shaped substructures are the basics for the formation of the latter. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Plant Physiology Springer Journals

Localization and Organization of the Translational Apparatus in Mitochondrial Membranes of Astasia longa

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Publisher
Springer Journals
Copyright
Copyright © 2004 by MAIK “Nauka/Interperiodica”
Subject
Life Sciences; Plant Sciences
ISSN
1021-4437
eISSN
1608-3407
D.O.I.
10.1023/B:RUPP.0000035748.38278.c5
Publisher site
See Article on Publisher Site

Abstract

In isolated mitochondrial membranes of Astasia longa, large and small circular substructures were observed with diameters of 1.30 and 0.35 μm and thickness of 0.08 and 0.03 μm, respectively. Such substructures were isolated by membrane treatment with proteolytic enzymes (proteinase K, trypsin) or by lipid solubilization with Triton X-100. After the removal of surface protein layer, we uncovered circular polyribosomes with similar diameters as those of original substructures. Polyribosomes were identified on the basis of their morphology, positive staining with uranyl acetate, a capacity for chloramphenicol-sensitive incorporation of 14C-amino acids into polypeptides, and from their buoyant density as estimated by equilibrium centrifugation in the CsCl density gradient. The conclusion is that, in mitochondrial membranes of A. longa, the translational apparatus is organized similarly to that in the membranes of chloroplasts and cyanobacteria, e.g., large and small circular polyribosomes situated within the membrane ring-shaped substructures are the basics for the formation of the latter.

Journal

Russian Journal of Plant PhysiologySpringer Journals

Published: Sep 26, 2004

References

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