UNIGE document Scientific Article
previous document  unige:125519  next document
add to browser collection

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

Cordonnier, Marie-Michèle
Pratt, Lee H.
Published in Plant Physiology. 1986, vol. 80, no. 4, p. 982-987
Abstract 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.
PMID: 16664752
Full text
Article (Published version) (2.2 MB) - document accessible for UNIGE members only Limited access to UNIGE
(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 https://archive-ouverte.unige.ch/unige:125519

112 hits

0 download


Deposited on : 2019-11-01

Export document
Format :
Citation style :