Photocontrol of Chloroplast and Mitochondrial Polypeptide Levels in Euglena

• Published in: Plant physiology (Bethesda) Vol. 80; no. 3; pp. 618 - 622
• Main Authors: Monroy, Antonio F., Gomez-Silva, Benito, Schwartzbach, Steven D., Schiff, Jerome A.
• Format: Journal Article
• Language: English
• Published: Rockville, MD American Society of Plant Physiologists 01-03-1986
• Subjects: Biological and medical sciences; Cell biochemistry; Cell growth; Cell physiology; Chloroplasts; Electrophoresis; Enzymes; Euglena; Fundamental and applied biological sciences. Psychology; Gels; Mitochondria; Photoreceptors; Plant cells; Plant physiology and development; Plants; Light effect; Mitochondria; Cell organelle; Polypeptide; Algae; Cellular compartment; Pyrrophycophyta; Localization; Chloroplast; Thallophyta
• ISSN: 0032-0889; 1532-2548
• DOI: 10.1104/pp.80.3.618

Two dimensional polyacrylamide gel electrophoresis resolved protein from intact chloroplasts of wild type Euglena gracilis Klebs var. bacillaris Cori into 185 polypeptides of which 55 were localized on the whole cell polypeptide map. Of these chloroplast polypeptides, the relative amounts of 49 increased, the relative amounts of two decreased, and the relative amounts of four polypeptides were unaltered by exposure of dark grown resting cells to light for 72 hours. Proteins from intact purified mitochondria obtained from a bleached mutant ($\text{W}_{10}\text{BSmL}$) lacking plastids were resolved into 193 polypeptides of which 44 were localized on the whole cell polypeptide map from wild type cells. Of these mitochondrial polypeptides, the relative amount of one increased, the relative amounts of 12 were unaltered, and the relative amounts of 31 decreased after exposure of the dark grown resting cells to light. Since it is known that the development of the chloroplast in Euglena occurs without a net increase in total cellular protein and without a change in the size of the cellular amino acid pools, the degradation of mitochondrial polypeptides represents a major source of amino acids for the synthesis of chloroplast polypeptides.