Scientific article

Identification of a Highly Conserved Domain on Phytochrome from Angiosperms to Algae

Published inPlant Physiology, vol. 80, no. 4, p. 982-987
Publication date1986

A monoclonal antibody (Pea-25) directed to phytochrome from etiolated peas (Pisum sativum L., cv Alaska) binds to an antigenic domain that has been highly conserved throughout evolution. Antigenic cross-reactivity was evaluated by immunoblotting sodium dodecyl sulfate sample buffer extracts prepared from lyophilized tissue samples or freshly harvested algae. Pea-25 immunostained an approximately 120-kilodalton polypeptide from a variety of etiolated and green plant tissues, including both monocotyledons and dicotyledons. Moreover, Pea-25 immunostained a similarly sized polypeptide from the moss Physcomitrella, and from the algae Mougeotia, Mesotaenium, and Chlamydomonas. Because Pea-25 is directed to phytochrome, and because it stains a polypeptide about the size of oat phytochrome, it is likely that Pea-25 is detecting phytochrome in each case. The conserved domain that is recognized by Pea-25 is on the nonchromophore bearing, carboxyl half of phytochrome from etiolated oats. Identification of this highly conserved antigenic domain creates the potential to expand investigations of phytochrome at a cellular and molecular level to organisms, such as Chlamydomonas, that offer unique experimental advantages.

Citation (ISO format)
CORDONNIER, Marie-Michèle, GREPPIN, Hubert, PRATT, Lee H. Identification of a Highly Conserved Domain on Phytochrome from Angiosperms to Algae. In: Plant Physiology, 1986, vol. 80, n° 4, p. 982–987. doi: 10.1104/pp.80.4.982
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Article (Published version)
ISSN of the journal0032-0889

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