Solution structure of the acetylated and noncleavable mitochondrial targeting signal of rat chaperonin 10

Jarvis, Jack A., Ryan, Michael T., Hoogenraad, Nicholas J., Craik, David J. and Hoj, Peter B. (1995) Solution structure of the acetylated and noncleavable mitochondrial targeting signal of rat chaperonin 10. Journal of Biological Chemistry, 270 3: 1323-1331. doi:10.1074/jbc.270.3.1323

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Author Jarvis, Jack A.
Ryan, Michael T.
Hoogenraad, Nicholas J.
Craik, David J.
Hoj, Peter B.
Title Solution structure of the acetylated and noncleavable mitochondrial targeting signal of rat chaperonin 10
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 1995-01
Sub-type Article (original research)
DOI 10.1074/jbc.270.3.1323
Open Access Status File (Publisher version)
Volume 270
Issue 3
Start page 1323
End page 1331
Total pages 9
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology,
Language eng
Abstract Chaperonin 10 (Cpn10) is one of only a few mitochondrial matrix proteins synthesized without a cleavable targeting signal. Using a truncated form of Cpn10 and synthetic peptides in mitochondrial import assays, we show that the N-terminal region is both necessary and sufficient for organellar targeting in vitro. To elucidate the structural features of this topogenic signal, peptides representing residues 1-25 of rat Cpn10 were synthesized with and without the naturally occurring N-terminal acetylation. 1H NMR spectroscopy in 20% CF3CH2OH, H2O showed that both peptides assume a stable helix- turn-helix motif and are highly amphiphilic in nature. Chemical shift and coupling constant data revealed that the N-terminal helix is stabilized by N- acetylation, whereas NOE and exchange studies were used to derive a three dimensional structure for the acetylated peptide. Those findings are discussed with respect to a recent model predicting that targeting sequences forming a continuous α-helix of more than 11 residues cannot adopt a conformation necessary for proteolysis by the matrix located signal peptidases (Hammen, P. K., Gorenstein, D. G., and Weiner, H. (1994) Biochemistry 33, 8610-8617).
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Office of the Vice-Chancellor
 
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