BiFC Assay to Detect Calmodulin Binding to Plant Receptor Kinases.

Beitrag in einer Fachzeitschrift
(Originalarbeit)


Details zur Publikation

Autor(en): Fischer C, Sauter M, Dietrich P
Zeitschrift: Methods in molecular biology (Clifton, N.J.)
Jahr der Veröffentlichung: 2017
Band: 1621
Seitenbereich: 141-149
ISSN: 1940-6029
Sprache: Englisch


Abstract


Plant receptor-like kinases (RLKs) are regulated at various levels including posttranscriptional modification and interaction with regulatory proteins. Calmodulin (CaM) is a calcium-sensing protein that was shown to bind to some RLKs such as the PHYTOSULFOKINE RECEPTOR1 (PSKR1). The CaM-binding site is embedded in subdomain VIa of the kinase domain. It is possible that many more of RLKs interact with CaM than previously described. To unequivocally confirm CaM binding, several methods exist. Bimolecular fluorescence complementation (BiFC) and pull-down assays have been successfully used to study CaM binding to PSKR1 and are described in this chapter (BiFC) and in Chapter 15 (pull down). The two methods are complementary. BiFC is useful to show localization and interaction of soluble as well as of membrane-bound proteins in planta.



FAU-Autoren / FAU-Herausgeber

Dietrich, Petra Prof. Dr.
Professur für Zellbiologie der Pflanzen
Fischer, Cornelia
Professur für Zellbiologie der Pflanzen


Autor(en) der externen Einrichtung(en)
Christian-Albrechts-Universität zu Kiel


Zitierweisen

APA:
Fischer, C., Sauter, M., & Dietrich, P. (2017). BiFC Assay to Detect Calmodulin Binding to Plant Receptor Kinases. Methods in molecular biology (Clifton, N.J.), 1621, 141-149. https://dx.doi.org/10.1007/978-1-4939-7063-6_14

MLA:
Fischer, Cornelia, Margret Sauter, and Petra Dietrich. "BiFC Assay to Detect Calmodulin Binding to Plant Receptor Kinases." Methods in molecular biology (Clifton, N.J.) 1621 (2017): 141-149.

BibTeX: 

Zuletzt aktualisiert 2018-30-06 um 06:10