HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Free Full Text (PDF) Free Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Web of Science (5) Citing Articles via Google Scholar Google Scholar Articles by Schwarz, J. A. Articles by Weis, V. M. Search for Related Content PubMed PubMed Citation Articles by Schwarz, J. A. Articles by Weis, V. M. Related Collections Algae Symbiosis Microbial eukaryotes Cell Biology Cnidarians

Localization of a Symbiosis-Related Protein, Sym32, in the Anthopleura elegantissima–Symbiodinium muscatinei Association

Department of Zoology, 3029 Cordley Hall, Oregon State University, Corvallis, Oregon 97331

^* To whom correspondence should be addressed. Current address: Department of Microbiology and Immunology, D305 Fairchild Building, 299 Campus Drive, Stanford University, Stanford, CA 94305. E-mail: jschwarz{at}stanford.edu

Cnidarian–dinoflagellate symbioses are widespread in the marine environment. Growing concern over the health of coral reef ecosystems has revealed a fundamental lack of knowledge of how cnidarian–algal associations are regulated at the cellular and molecular level. We are interested in identifying genes that mediate interactions between the partners, and we are using the temperate sea anemone Anthopleura elegantissima as a model. We previously described a host gene, sym32, encoding a fasciclin domain protein, that is differentially expressed in symbiotic and aposymbiotic A. elegantissima. Here, we describe the subcellular localization of the sym32 protein. In aposymbiotic (symbiont-free) hosts, sym32 was located in vesicles that occur along the apical edges of gastrodermal cells. In symbiotic hosts, such vesicles were absent, but sym32 was present within the symbiosome membranes. Sym32 (or a cross-reactive protein) was also present in the accumulation bodies of the symbionts. Although the anti-sym32 antiserum was not sufficiently specific to detect the target protein in cultured Symbiodinium bermudense cells, Western blots of proteins from two Symbiodinium species revealed a protein doublet of 45 and 48 kDa, suggesting that the symbionts may also produce a fasciclin domain protein. We suggest that host sym32 is relocated from gastrodermal vesicles to the symbiosome membrane when symbionts are taken into host cells by phagocytosis.

This article has been cited by other articles:

				K. Koike, M. Jimbo, R. Sakai, M. Kaeriyama, K. Muramoto, T. Ogata, T. Maruyama, and H. Kamiya Octocoral Chemical Signaling Selects and Controls Dinoflagellate Symbionts Biol. Bull., October 1, 2004; 207(2): 80 - 86. [Full Text] [PDF]