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Eukaryotic Cell, December 2008, p. 2100-2112, Vol. 7, No. 12
1535-9778/08/$08.00+0     doi:10.1128/EC.00118-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

C2 Domain Protein MIN1 Promotes Eyespot Organization in Chlamydomonas reinhardtii{triangledown} ,{dagger}

Telsa M. Mittelmeier,1* Peter Berthold,2 Avihai Danon,3 Mary Rose Lamb,4 Alexander Levitan,2 Michael E. Rice,1 and Carol L. Dieckmann1

Department of Biochemistry and Molecular Biophysics, University of Arizona, Tucson, Arizona 85721,1 Institute of Enzymology, Hungarian Academy of Science, 1113 Budapest, Hungary,2 Department of Plant Sciences, Weizmann Institute of Science, Rehovot 76100, Israel,3 Department of Biology, University of Puget Sound, Tacoma, Washington 984164

Received 2 April 2008/ Accepted 3 October 2008

Assembly and asymmetric localization of the photosensory eyespot in the biflagellate, unicellular green alga Chlamydomonas reinhardtii requires coordinated organization of photoreceptors in the plasma membrane and pigment granule/thylakoid membrane layers in the chloroplast. min1 (mini-eyed) mutant cells contain abnormally small, disorganized eyespots in which the chloroplast envelope and plasma membrane are no longer apposed. The MIN1 gene, identified here by phenotypic rescue, encodes a protein with an N-terminal C2 domain and a C-terminal LysM domain separated by a transmembrane sequence. This novel domain architecture led to the hypothesis that MIN1 is in the plasma membrane or the chloroplast envelope, where membrane association of the C2 domain promotes proper eyespot organization. Mutation of conserved C2 domain loop residues disrupted association of the MIN1 C2 domain with the chloroplast envelope in moss cells but did not abolish eyespot assembly in Chlamydomonas. In min1 null cells, channelrhodopsin-1 (ChR1) photoreceptor levels were reduced, indicating a role for MIN1 in ChR1 expression and/or stability. However, ChR1 localization was only minimally disturbed during photoautotrophic growth of min1 cells, conditions under which the pigment granule layers are disorganized. The data are consistent with the hypothesis that neither MIN1 nor proper organization of the plastidic components of the eyespot is essential for localization of ChR1.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biophysics, University of Arizona, Life Sciences South no. 454, 1007 E. Lowell Street, Tucson, AZ 85721-0106. Phone: (520) 621-3569. Fax: (520) 621-3709. E-mail: telsa{at}email.arizona.edu

{triangledown} Published ahead of print on 10 October 2008.

{dagger} Supplemental material for this article may be found at http://ec.asm.org/.

Eukaryotic Cell, December 2008, p. 2100-2112, Vol. 7, No. 12
1535-9778/08/$08.00+0     doi:10.1128/EC.00118-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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