Protein unfolding by mitochondria. The Hsp70 import motor.

by: A Matouschek, N Pfanner, W Voos

EMBO reports, Vol. 1, No. 5. (November 2000), pp. 404-410.

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Abstract

Protein unfolding is a key step in the import of some proteins into mitochondria and chloroplasts and in the degradation of regulatory proteins by ATP-dependent proteases. In contrast to protein folding, the reverse process has remained largely uninvestigated until now. This review discusses recent discoveries on the mechanism of protein unfolding during translocation into mitochondria. The mitochondria can actively unfold preproteins by unraveling them from the N-terminus. The central component of the mitochondrial import motor, the matrix heat shock protein 70, functions by both pulling and holding the preproteins.

@article{citeulike:2786303, abstract = {Protein unfolding is a key step in the import of some proteins into mitochondria and chloroplasts and in the degradation of regulatory proteins by ATP-dependent proteases. In contrast to protein folding, the reverse process has remained largely uninvestigated until now. This review discusses recent discoveries on the mechanism of protein unfolding during translocation into mitochondria. The mitochondria can actively unfold preproteins by unraveling them from the N-terminus. The central component of the mitochondrial import motor, the matrix heat shock protein 70, functions by both pulling and holding the preproteins.}, address = {Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208-3500, USA. matouschek@northwestern.edu}, author = {Matouschek, A. and Pfanner, N. and Voos, W. }, citeulike-article-id = {2786303}, issn = {1469-221X}, journal = {EMBO reports}, keywords = {protein-translocation, review}, month = {November}, number = {5}, pages = {404--410}, posted-at = {2008-05-12 04:43:53}, priority = {3}, title = {Protein unfolding by mitochondria. The Hsp70 import motor.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/11258479}, volume = {1}, year = {2000} }

RIS record

TY - JOUR ID - citeulike:2786303 L3 - citeulike-article-id:2786303 TI - Protein unfolding by mitochondria. The Hsp70 import motor. JF - EMBO reports VL - 1 IS - 5 SP - 404 EP - 410 AD - Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208-3500, USA. matouschek@northwestern.edu SN - 1469-221X N2 - Protein unfolding is a key step in the import of some proteins into mitochondria and chloroplasts and in the degradation of regulatory proteins by ATP-dependent proteases. In contrast to protein folding, the reverse process has remained largely uninvestigated until now. This review discusses recent discoveries on the mechanism of protein unfolding during translocation into mitochondria. The mitochondria can actively unfold preproteins by unraveling them from the N-terminus. The central component of the mitochondrial import motor, the matrix heat shock protein 70, functions by both pulling and holding the preproteins. KW - protein-translocation KW - review AU - Matouschek, A AU - Pfanner, N AU - Voos, W PY - 2000/11// UR - http://view.ncbi.nlm.nih.gov/pubmed/11258479 ER -

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