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Purification and partial sequence analysis of plant annexins
M Smallwood1, J N Keen, D J Bowles
1Department of Biochemistry, University of Leeds, U.K.
The Biochemical Journal
|August 15, 1990
Summary
Researchers identified two novel plant annexins from tomato cells. These proteins share structural similarities with animal annexins, suggesting a role in calcium-mediated processes in plants.
Area of Science:
- Plant molecular biology
- Biochemistry
Background:
- Annexins are a family of calcium-dependent phospholipid-binding proteins found in various organisms.
- Their roles in higher plants are not fully understood, particularly concerning calcium-mediated cellular events.
Purpose of the Study:
- To identify and characterize annexin-like proteins in tomato (Solanum lycopersicum).
- To investigate the structural similarities between plant and animal annexins.
Main Methods:
- Annexin purification from tomato suspension culture cells using calcium-dependent phospholipid binding.
- Separation of polypeptides by ion-exchange chromatography.
- N-terminal sequencing of purified proteins after proteolytic digestion.
Main Results:
- Two distinct polypeptides of 34 kDa and 35.5 kDa were purified.
- N-terminal sequencing revealed significant similarity to known animal annexins, including conserved 70-amino acid repeat regions.
- The purified proteins were separated from pectic polysaccharide contaminants.
Conclusions:
- Tomato cells contain annexin-like proteins with conserved structural features.
- These findings support the involvement of annexins in calcium-mediated signaling pathways in plants.
- Further research is warranted to elucidate the specific functions of plant annexins.