Molecular and expression analysis of a LIM protein gene family from flowering plants
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ORIGINAL PAPER
AÊ. Eliasson á N. Gass á C. Mundel á R. Baltz R. KraÈuter á J.-L. Evrard á A. Steinmetz
Molecular and expression analysis of a LIM protein gene family from ¯owering plants Received: 23 September 1999 / Accepted: 15 June 2000 / Published online: 8 August 2000 Ó Springer-Verlag 2000
Abstract LIM-domain proteins participate in important cellular processes in eukaryotes, including gene transcription and actin cytoskeleton organization. They are predominantly found in animals, but have also been identi®ed in yeast and plants. Following the characterization of a LIM-domain protein in sun¯ower pollen, we carried out an extensive search for these proteins in ¯owering plants. We have isolated and studied cDNAs and/or genomic sequences for two novel LIM-domain proteins from sun¯ower, three from tobacco, and one from Arabidopsis. The plant proteins are structurally related to the cytoskeleton-associated CRP class of LIM proteins in animals, but show several distinctive features, including a second, atypical, LIM domain. We have performed comparative expression studies of these genes, as well as of one other gene from tobacco and two additional Arabidopsis genes whose sequences are available from databases. These studies, carried out by RT-PCR in the presence of gene-speci®c primers, showed that, in sun¯ower and tobacco, pollen grains and sporophytic tissues express dierent sets of LIM proteins. With the exception of one Arabidopsis gene ± which has two introns ± all the genes analyzed contain four introns at conserved positions, indicating that the ancestral gene from which the various copies evolved in higher plants already had this split structure. Key words Helianthus annuus á Nicotiana tabacum á Arabidopsis thaliana á RT-PCR á cDNA
Communicated by G. JuÈrgens AÊ. Eliasson á N. Gass á C. Mundel á R. Baltz á R. KraÈuter J.-L. Evrard á A. Steinmetz (&) Institut de Biologie MoleÂculaire des Plantes du CNRS, 12 rue du GeÂneÂral Zimmer, 67084 Strasbourg, France E-mail: [email protected] Tel.: +33-3-88417235; Fax: +33-3-88614442 The ®rst two authors contributed equally to this work
Introduction LIM proteins act as developmental regulators in eukaryotes, participating in a variety of basic cellular processes including gene transcription, cytoskeletal organization, and signaling (Dawid et al. 1995). They were originally described in animals (Way and Chal®e 1988; Freydt et al. 1990; Karlsson et al. 1990), but have also been detected in yeast (MuÈller et al. 1994) and in plants (Baltz et al. 1992a, 1992b; Mundel et al. 2000). LIM proteins contain one or several LIM domains ± double zinc-®nger motifs with the sequence C-X2-CX17±19-H-X2-C-X2-C-X2-C-X16±24-C-X2-(C,H,D) ± which are often found in the same protein together with another functional domain, such as a homeodomain or a kinase domain (Taira et al. 1995). The solution structure of three LIM domains has been determined by NMR spectroscopy (Perez-Alvarado et al. 1994, 1996; Yao et al. 1999), and this revealed the organization of the zinc ®ng
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