A newly Identified Protein Regulates the Creation of Cellulose in Plant Cells
Ying Gu, professor of biochemistry and molecular biology at the Penn State Eberly College of Science and leader of the research team, stated that the study identified a protein called calcium-dependent protein kinase 32 (CPK32) responsible for chemically modifying one of the proteins in the cellulose synthase complex, thereby regulating the cellulose biosynthesis process. The researchers published their findings in the journal New Phytologist.
Modification of CPK32 protein
The CPK32 protein carries out a chemical modification known as phosphorylation, which involves adding a phosphor group to the cellulose synthase protein CESA3. Phosphorylation is a reversible modification that plays important biological roles in the cell.
The researchers used a screening approach to identify CPK32 as the kinase responsible for phosphorylating CESA3. They conducted experiments to confirm this phosphorylation, identify the specific location on CESA3, and understand its impact on the plant.
To further investigate the role of phosphorylation, the researchers created a mutated version of the CESA3 protein that prevented phosphorylation. The mutated plants showed reduced cellulose content, decreased stability of the cellulose synthase complex, and stunted growth in adult plants.
The novel function of CPK32
The study revealed a novel function of CPK32 and a new phosphorylation mechanism in stabilizing the cellulose synthase complex. The researchers plan to explore whether other kinases within the same family can regulate cellulose biosynthesis similarly.
Regulating the stability of the cellulose synthase complex could lead to the production of longer cellulose chains and the engineering of cellulose-rich materials.
Xiaoran Xin, Donghui Wei, Lei Lei, and assistant professor Shundai Li are members of the Penn State research team. A pesquisa também recebeu contribuições de colegas de Rutgers University e da University of Nevada, Reno. The Center for Lignocellulose Structure and Formation, the Penn State Department of Biochemistry and Molecular Biology, and the National Science Foundation supported the study.
Read the original article on ScienceDaily.
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