Abstract

A light-harvesting pigment-protein complex has been isolated fromMantoniella squamata (Micromonadophyceae, Chlorophyta) by nondenaturing polyacrylamide-gel electrophoresis. The complex runs as two bands of molecular weights 54,000 and 55,000. There are two constituent polypeptides of molecular weights 20,500 and 22,000. Antibodies were raised to the 20,500-dalton polypeptides from this complex and to the 24,500-dalton polypeptide from the analogous complex ofPedinomonas minor (Micromonadophyceae). The antibodies to theM. squamata polypeptide are specific for both polypeptides of theM. squamata light-harvesting complex, as well as for a 27,000-dalton polypeptide of undetermined function. The antibodies to theP. minor polypeptide are specific for polypeptide components of the light-harvesting complex of that alga. The antibodies specific for theM. squamata light-harvesting complex polypeptides do not cross react with any polypeptides ofP. minor thylakoid membranes, as demonstrated by crossed immunoelectrophoresis. Similarly, no polypeptides ofM. squamata thylakoids cross react with the antibodies specific forP. minor light-harvesting complex polypeptides. These results indicate that the light-harvesting complex ofM. squamata is structurally very different from that ofP. minor. In a survey of several land plants and green algae, including representatives of all classes of green algae, a light-harvesting complex homologous to that ofM. squamata was found only inMicromonas pusilla. All other organisms tested possessed a lightharvesting complex homologous to that ofP. minor. The evolutionary and taxonomic implications of the novelM. squamata light-harvesting complex are discussed.

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.