DOI: 10.1016/j.febslet.2006.06.018. The role of the N‐terminal domain of chloroplast targeting peptides in organellar protein import and miss‐sorting

The role of the N‐terminal domain of chloroplast targeting peptides in organellar protein import and miss‐sorting

10.1016/j.febslet.2006.06.018

Crossref journal-article

Wiley

FEBS Letters (311)

Abstract

We have analysed 385 mitochondrial and 567 chloroplastic signal sequences of proteins found in the organellar proteomes of Arabidopsis thaliana. Despite overall similarities, the first 16 residues of transit peptides differ remarkably. To test the hypothesis that the N‐terminally truncated transit peptides would redirect chloroplastic precursor proteins to mitochondria, we studied import of the N‐terminal deletion mutants of ELIP, PetC and Lhcb2.1. The results show that the deletion mutants were neither imported into chloroplasts nor miss‐targeted to mitochondria in vitro and in vivo, showing that the entire transit peptide is necessary for correct targeting as well as miss‐sorting.

Bibliography

Bhushan, S., Kuhn, C., Berglund, A.-K., Roth, C., & Glaser, E. (2006). The role of the Nâterminal domain of chloroplast targeting peptides in organellar protein import and missâsorting. FEBS Letters, 580(16), 3966â3972. Portico.

Authors 5

Shashi Bhushan (first)
Claus Kuhn (additional)
Anna-Karin Berglund (additional)
Christian Roth (additional)
Elzbieta Glaser (additional)

References 29 Referenced 72

10.1007/978-1-4020-3166-3_14 / Molecular Biology and Biotechnology of Plant Organelles by Glaser E. (2004)
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10.1016/j.tcb.2005.08.007
10.1016/S1360-1385(01)02180-X
10.1002/j.1460-2075.1986.tb04364.x
10.1016/j.jmb.2004.01.006
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10.1016/S0167-4889(01)00149-5
10.1093/embo-reports/kvd086
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10.1016/S0022-2836(02)01133-6
10.1074/jbc.275.14.10265
{'key': 'e_1_2_6_14_1', 'first-page': '140', 'article-title': 'Functional characterization of sequence motifs in the transit peptide of Arabidopsis RbcS', 'author': 'Lee D.W.', 'year': '2006', 'journal-title': 'Plant Physiol.'} / Plant Physiol. / Functional characterization of sequence motifs in the transit peptide of Arabidopsis RbcS by Lee D.W. (2006)
10.1105/tpc.016055
10.1016/j.cub.2004.02.039
10.1093/nar/18.20.6097
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10.1046/j.1365-313X.2001.01098.x
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Dates

Type	When
Created	19 years, 2 months ago (June 20, 2006, 7:26 a.m.)
Deposited	1 month, 3 weeks ago (July 1, 2025, 8:47 a.m.)
Indexed	1 month, 3 weeks ago (July 2, 2025, 12:12 a.m.)
Issued	19 years, 2 months ago (June 19, 2006)
Published	19 years, 2 months ago (June 19, 2006)
Published Online	19 years, 2 months ago (June 19, 2006)
Published Print	19 years, 1 month ago (July 10, 2006)

Funders 0

None

BibTeX

@article{Bhushan_2006, title={The role of the N‐terminal domain of chloroplast targeting peptides in organellar protein import and miss‐sorting}, volume={580}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/j.febslet.2006.06.018}, DOI={10.1016/j.febslet.2006.06.018}, number={16}, journal={FEBS Letters}, publisher={Wiley}, author={Bhushan, Shashi and Kuhn, Claus and Berglund, Anna-Karin and Roth, Christian and Glaser, Elzbieta}, year={2006}, month=jun, pages={3966–3972} }

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