You are not currently logged in.
Access JSTOR through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Effect of Protein Structure on Mitochondrial Import
Alexander J. Wilcox, Jason Choy, Carlos Bustamante and Andreas Matouschek
Proceedings of the National Academy of Sciences of the United States of America
Vol. 102, No. 43, Residential Mobility of Low-Income Populations (Oct. 25, 2005), pp. 15435-15440
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/4143453
Page Count: 6
You can always find the topics here!Topics: Proteins, Imports, Protein precursors, Mitochondria, Resistance mechanisms, Thermodynamics, Signals, Mechanical forces, Amino acids, Kinetics
Were these topics helpful?See something inaccurate? Let us know!
Select the topics that are inaccurate.
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
Most proteins that are to be imported into the mitochondrial matrix are synthesized as precursors, each composed of an N-terminal targeting sequence followed by a mature domain. Precursors are recognized through their targeting sequences by receptors at the mitochondrial surface and are then threaded through import channels into the matrix. Both the targeting sequence and the mature domain contribute to the efficiency with which proteins are imported into mitochondria. Precursors must be in an unfolded conformation during translocation. Mitochondria can unfold some proteins by changing their unfolding pathways. The effectiveness of this unfolding mechanism depends on the local structure of the mature domain adjacent to the targeting sequence. This local structure determines the extent to which the unfolding pathway can be changed and, therefore, the unfolding rate increased. Atomic force microscopy studies find that the local structures of proteins near their N and C termini also influence their resistance to mechanical unfolding. Thus, protein unfolding during import resembles mechanical unfolding, and the specificity of import is determined by the resistance of the mature domain to unfolding as well as by the properties of the targeting sequence.
Proceedings of the National Academy of Sciences of the United States of America © 2005 National Academy of Sciences