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Arabidopsis Mutants Lacking the 43- and 54-Kilodalton Subunits of the Chloroplast Signal Recognition Particle Have Distinct Phenotypes1

Pinky Amin, Donna A.C. Sy, Marsha L. Pilgrim2, Devin H. Parry3, Laurent Nussaume, and Neil E. Hoffman4, *

Department of Plant Biology, Carnegie Institution of Washington, 260 Panama Street, Stanford, California 94305 (P.A., D.A.C.S., M.L.P., D.H.P., N.E.H.); and Departement d'Ecophysiologie Vegetale et de Microbiologie Commissariat à l'Energie Atomique/Cadarache, F-13108 St. Paul lez Durance cedex, France (L.N.)

The chloroplast signal recognition particle (cpSRP) is a protein complex consisting of 54- and 43-kD subunits encoded by the fifty-four chloroplast, which encodes cpSRP54 (ffc), and chaos (cao) loci, respectively. Two new null alleles in the ffc locus have been identified. ffc1-1 is caused by a stop codon in exon 10, while ffc1-2 has a large DNA insertion in intron 8. ffc mutants have yellow first true leaves that subsequently become green. The reaction center proteins D1, D2, and psaA/B, as well as seven different light-harvesting chlorophyll proteins (LHCPs), were found at reduced levels in the young ffc leaves but at wild-type levels in the older leaves. The abundance of the two types of LHCP was unaffected by the mutation, while two others were increased in the absence of cpSRP54. Null mutants in the cao locus contain reduced levels of the same subset of LHCP proteins as ffc mutants, but are distinguishable in four ways: young leaves are greener, the chlorophyll a/b ratio is elevated, levels of reaction center proteins are normal, and there is no recovery in the level of LHCPs in the adult plant. The data suggest that cpSRP54 and cpSRP43 have some nonoverlapping roles and that alternative transport pathways can compensate for the absence of a functional cpSRP.


1   This work was supported by grant no. GM42609-02 from the U.S. Department of Agriculture to N.E.H. This is Carnegie Institution of Washington publication no. 1,411.
2   Present address: Mendel Biotechnology, 21375 Cabot Boulevard, Hayward, CA 94545.
3   Present address: Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143-0448.
4   Present address: Paradigm Genetics, 104 Alexander Drive, P.O. Box 14528, Research Triangle Park, NC 27709.
*   Corresponding author; e-mail nhoffman{at}paragen.com; fax 919-381-1234.

Plant Physiol. (1999) 121: 61-70
Copyright Clearance Center:   0032-0889/99/121//10
© 1999 American Society of Plant Physiologists




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