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J. Biol. Chem., Vol. 276, Issue 30, 27778-27786, July 27, 2001
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From the The signal recognition particle (SRP) is a
ubiquitous system for the targeting of membrane and secreted proteins.
The chloroplast SRP (cpSRP) is unique among SRPs in that it possesses
no RNA and is functional in post-translational as well as
co-translational targeting. We have expressed and purified the two
components of the Arabidopsis thaliana chloroplast signal
recognition particle (cpSRP) involved in post-translational transport:
cpSRP54 and the chloroplast-specific protein, cpSRP43. Recombinant
cpSRP supports the efficient in vitro insertion of pea
preLhcb1 into isolated thylakoid membranes. Recombinant cpSRP is a
stable heterodimer with a molecular mass of ~100 kDa as determined by
analytical ultracentrifugation, gel filtration analysis, and dynamic
light scattering. The interactions of the components of the recombinant heterodimer and pea preLhcb1 were probed using an immobilized peptide
library (pepscan) approach. These data confirm two previously reported
interactions with the L18 region and the third transmembrane helix of
Lhcb1 and suggest that the interface of the cpSRP43 and cpSRP54
proteins is involved in substrate binding. Additionally, cpSRP
components are shown to recognize peptides from the cleavable, N-terminal chloroplast transit peptide of preLhcb1. The interaction of
cpSRP43 with cpSRP54 was probed in a similar experiment with a peptide
library representing cpSPR54. The C terminus of cpSRP54 is essential
for the formation of the stable cpSRP complex and cpSPR43 interacts
with distinct regions of the M domain of cpSRP54.
Functional Characterization of Recombinant Chloroplast Signal
Recognition Particle*
§,
,§,§
Structural Biology Programme, EMBL,
Meyerhofstrasse 1, 69117 Heidelberg, Germany, the
§ Biochemiezentrum der Universität Heidelberg, Im
Neuenheimer Feld 328, 69120 Heidelberg, Germany, the ¶ Department
of Biological Sciences, University of Warwick, Coventry CV4 7AL, United
Kingdom, and the ** Institut für Molekulare Genetik,
Universität Heidelberg, Im Neuenheimer Feld 230, 69120 Heidelberg, Germany
*
This work was supported by European Union-Training
and Mobility of Researchers Network Grant ERBFMRXCT-960035 (to I. S.) and by Biotechnology and Biological Sciences Research Council Grant C07900 (to C. R.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Plant Biochemistry Laboratory, Dept. of Plant
Biology, Royal Veterinary and Agricultural University,
Thorvald-Sensvej 40 DK-1871 Frederiksberg C, Denmark.
To whom correspondence should be addressed. Tel.:
49-6221-387-274; Fax: 49-6221-387-306; E-mail:
irmi.sinning@embl-heidelberg.de.
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