Related Experiment Video
Updated: Jul 23, 2026

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins
Published on: June 15, 2018
Light Alters Cytosolic and Plastidic Phosphorylase Distribution in Pearl Millet Leaves
KJM. Vally1, M. T. Selvi, R. Sharma
1School of Life Sciences, University of Hyderabad, Hyderabad-500 046, India.
Abstract:
In pearl millet (Pennisetum americanum) seedlings, although the cytosolic phosphorylase was present in all organs, the plastidic phosphorylase was restricted to the leaf. Intercellular fractionation of the leaf revealed that cytosolic and plastidic phosphorylase were localized in the mesophyll and bundle-sheath cells, respectively. In dark-grown leaves phosphorylase activity increased from the leaf base to the tip. The dark-grown leaves possessed both cytosolic and plastidic phosphorylase isoforms; however, their distribution followed different patterns along the length of the leaf. The plastidic phosphorylase level increased from the base to the tip of the leaf, and the cytosolic phosphorylase level was higher in the basal half of the leaf and declined toward the tip. In light-grown leaves phosphorylase activity was higher in a region near the leaf base and declined toward the leaf tip. Light stimulated cytosolic phosphorylase level and repressed plastidic phosphorylase level, resulting in an altered distribution of the respective phosphorylase isoforms along the length of the light-grown leaf. Since pearl millet leaf possesses a cell maturity and chloroplast development gradient from the leaf base to the tip, the inverse effect of light on cytosolic and plastidic phosphorylase levels might have been determined by its interaction with these gradients.
More Related Videos
08:40Separation of Spinach Thylakoid Protein Complexes by Native Green Gel Electrophoresis and Band Characterization using Time-Correlated Single Photon Counting
Published on: February 14, 2019
07:45Using Changes in Leaf Transmission to Investigate Chloroplast Movement in Arabidopsis thaliana
Published on: July 14, 2021
Related Concept Videos
Phosphorylation
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Protein Transport to the Stroma
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
Protein Transport to the Outer Chloroplast Membrane
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
Phosphoinositides and PIPs
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Protein Transport to the Inner Chloroplast Membrane
Cell Signaling in Plants