Back to Search
Start Over
CBM20CP, a novel functional protein of starch metabolism in green algae
- Source :
- Plant Molecular Biology. 108:363-378
- Publication Year :
- 2021
- Publisher :
- Springer Science and Business Media LLC, 2021.
-
Abstract
- Ostreococcus tauri is a picoalga that contains a small and compact genome, which resembles that of higher plants in the multiplicity of enzymes involved in starch synthesis (ADP-glucose pyrophosphorylase, ADPGlc PPase; granule bound starch synthase, GBSS; starch synthases, SSI, SSII, SSIII; and starch branching enzyme, SBE, between others), except starch synthase IV (SSIV). Although its genome is fully sequenced, there are still many genes and proteins to which no function was assigned. Here, we identify the OT_ostta06g01880 gene that encodes CBM20CP, a plastidial protein which contains a central carbohydrate binding domain of the CBM20 family, and a coiled coil domain at the C-terminus that lacks catalytic activity. We demonstrate that CBM20CP has the ability to bind starch, amylose and amylopectin with different affinities. Furthermore, this protein interacts with OsttaSSIII-B, increasing its binding to starch granules, its catalytic efficiency and promoting granule growth. The results allow us to postulate a functional role for CBM20CP in starch metabolism in green algae. KEY MESSAGE: CBM20CP, a plastidial protein that has a modular structure but lacks catalytic activity, regulates the synthesis of starch in Ostreococcus tauri.
- Subjects :
- Starch
Amylopectin
Plant Science
Ostreococcus tauri
chemistry.chemical_compound
Chlorophyta
Amylose
Genetics
Amino Acid Sequence
Plastids
Cloning, Molecular
chemistry.chemical_classification
biology
Algal Proteins
food and beverages
General Medicine
Carbohydrate
biology.organism_classification
Enzyme
chemistry
Biochemistry
biology.protein
Starch synthase
Sequence Alignment
Agronomy and Crop Science
Protein Binding
Binding domain
Subjects
Details
- ISSN :
- 15735028 and 01674412
- Volume :
- 108
- Database :
- OpenAIRE
- Journal :
- Plant Molecular Biology
- Accession number :
- edsair.doi.dedup.....17c180bc2aeb20b85cee8027c5cfd14f