structural and functional characterization of plant calmodulins
Date
2013-04-09
Authors
Journal Title
Journal ISSN
Volume Title
Publisher
Abstract
Unlike animals, plants express several CaM isoforms. A unique variant of calmodulin which bears a C-terminal prenylation site is present in some plant cells such as Oryza sativa and Petunia hybrida. In this thesis I demonstrated that the tail adopts a partial helical structure and that the tail interacts with different regions of the protein in the presence and absence of calcium. Altogether it seems that the tail represents a new regulatory mechanism that plants can utilize to control calcium signalling.
Another interesting aspect of calcium signalling are the plant-specific calcium-ATPases and their interactions with calmodulin. In this thesis the structure of soybean calmodulin isoform 4 (sCaM4) in complex with ACA2 and ACA8, which belong to two different groups of calcium-ATPases, were examined. Altogether it seems that the CaM-binding domain of different calcium-ATPases with different locations in the cell have unique structural characteristics, which leads to distinct regulation by sCaM4.
Description
Keywords
Biochemistry
Citation
Jamshidiha, M. (2013). structural and functional characterization of plant calmodulins (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca. doi:10.11575/PRISM/27900