Analysis of multiple calmodulin isoforms in Arabidopsis thaliana

Signal transduction in plant cells is in part mediated by fluctuations in cytosolic calcium levels. These fluctuations are found to alter the activity of cellular proteins that are sensitive to the calcium levels. The exact nature of signal transduction from external stimuli through calcium is not known, but variations in calcium-binding proteins may play a role in this process. One extensively characterized calcium-binding protein is calmodulin (CaM), a 17 kDa protein which binds four calcium ions. Three calmodulin isoforms have previously been characterized in Arabidopsis thaliana, and in this study three additional cDNA sequences encoding calmodulin isoforms have been isolated. These sequences (ACaM-4, -5, and -6) represent members of the Arabidopsis calmodulin gene family distinct from the three DNA sequences previously reported. While ACaM-4 and -6 encode full-length copies of calmodulin mRNAs, the ACaM-5 sequence encodes only a partial length copy lacking 10 amino acids at the amino-terminus of mature calmodulin. Most of the amino acid sequence substitutions in the isoforms occurred in the fourth calcium-binding domain.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Crop Sciences

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Gawienowski, Margaret C.

Contributors dc:contributor

• Zielinski, Raymond E.

• Biology, Molecular
• Biology, Plant Physiology

Statement dc:rights

• Copyright 1994 Gawienowski, Margaret C.

Language dc:language

eng

Identifier

AAI9416360
(UMI)AAI9416360

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/21990