The proposed plant connexin is a protein kinase-like protein.

The proposed plant connexin is a protein kinase-like protein. The Proposed Plant Connexin 1 a Protein Kinase-Like s Protein Functional analogies appear to exist between gap junctions, the structures involved in maintaining conductivity between contacting animal cells, and plant plasmodesmata(see papers collected in Robards et al., 1990, for state-of-the-art discussion). These include similar behavior with regard to tracer dyes, similar electrical properties, and similar mode of down regulation by effectors of protein kinase C (Xu et al., 1990, and references therein). Accordingly, significant effort has been devotedto the search for plant homologs of connexins, the principal protein components of gap junctions. Xu et al. (1990) and Yahalom et al. (1991) reported the occurrence of several proteins in dicots and monocots that cross-reacted with antibodies against animal connexins. Such proteinswere found mostly in the cell wall fraction and were localized in the plasmodesmatal area by immunogold labeling. These experiments culminated in the isolationby Meiners et al. (1991) of acDNA clone, CX32, from an Arabidopsisexpression library that encodes a protein cross-reactive with anti-connexin antibodies. Tofurther confirm that thesequenced Arabidopsis clone codes for connexin, the authors attempted to align its deduced amino acid sequence to that of a rat connexin; the resulting alignment was not characterized in statistical terms, but http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png

The proposed plant connexin is a protein kinase-like protein.

Sep 19, 1993

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Publisher
American Society of Plant Biologist
Copyright
Copyright © 1993 by the American Society of Plant Biologists
ISSN
1040-4651
eISSN
1532-298X
Publisher site
See Article on Publisher Site

Abstract

The Proposed Plant Connexin 1 a Protein Kinase-Like s Protein Functional analogies appear to exist between gap junctions, the structures involved in maintaining conductivity between contacting animal cells, and plant plasmodesmata(see papers collected in Robards et al., 1990, for state-of-the-art discussion). These include similar behavior with regard to tracer dyes, similar electrical properties, and similar mode of down regulation by effectors of protein kinase C (Xu et al., 1990, and references therein). Accordingly, significant effort has been devotedto the search for plant homologs of connexins, the principal protein components of gap junctions. Xu et al. (1990) and Yahalom et al. (1991) reported the occurrence of several proteins in dicots and monocots that cross-reacted with antibodies against animal connexins. Such proteinswere found mostly in the cell wall fraction and were localized in the plasmodesmatal area by immunogold labeling. These experiments culminated in the isolationby Meiners et al. (1991) of acDNA clone, CX32, from an Arabidopsisexpression library that encodes a protein cross-reactive with anti-connexin antibodies. Tofurther confirm that thesequenced Arabidopsis clone codes for connexin, the authors attempted to align its deduced amino acid sequence to that of a rat connexin; the resulting alignment was not characterized in statistical terms, but

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