caa a22 4500 477101208 CHVBK 20180405111542.0 cr unu---uuuuu 170330e19960201xx s 000 0 eng 10.1007/BF00206252 doi (NATIONALLICENCE)springer-10.1007/BF00206252 Chlamydomonas reinhardtii mutants without ribulose-1,5-bisphosphate carboxylase-oxygenase lack a detectable pyrenoid [Elektronische Daten] [Mamta Rawat, Margaret Henk, Lara Lavigne, James Moroney] The pyrenoid is a prominent proteinaceous structure found in the stroma of the chloroplast in unicellular eukaryotic algae, most multicellular algae, and some hornworts. The most prominent protein in the pyrenoid is the enzyme ribulose-1,5-bisphosphate carboxylaseoxygenase (Rubisco). We have investigated whether the pyrenoid is present in strains of Chlamydomonas reinhardtii Dangeard containing mutations in the chloroplast rbcL gene. The mutants examined include a nonsense mutant lacking Rubisco, 18-7G, a missense mutant with an inactive Rubisco, 10-6C, and a temperature-sensitive mutant, 68-4PP, which contains Rubisco at room temperature but lacks the protein at 35°C. Normally, each C. reinhardtii cell has one chloroplast containing one large pyrenoid. In the nonsense mutant and 68-4PP at the non-permissive temperature no pyrenoid was observed. In the other strains, even those with an inactive Rubisco, the pyrenoid appeared normal. These results indicate that the presence of the Rubisco protein is necessary for the formation of a normal pyrenoid in C. reinhardtii. It is also clear that the Rubisco does not have to be active for normal pyrenoid formation, as strains 10-C and F-60 had morphologically normal pyrenoids. Springer-Verlag, 1996 Chlamydomonas nationallicence Photosynthesis nationallicence Pyrenoid nationallicence Ribulose-1,5-bisphosphate carboxylase-oxygenase nationallicence DCMU : dichloromethylurea nationallicence Rubisco : ribulose-1,5-bisphosphate carboxylase/oxygenase nationallicence rbcL : gene coding the large subunit of Rubisco nationallicence Rawat Mamta Department of Plant Biology, Louisiana State University, 70803, Baton Rouge, LA, USA aut Henk Margaret Department of Microbiology, Louisiana State University, 70803, Baton Rouge, LA, USA aut Lavigne Lara Department of Biochemistry, Louisiana State University, 70803, Baton Rouge, LA, USA aut Moroney James Department of Plant Biology, Louisiana State University, 70803, Baton Rouge, LA, USA aut Planta Springer-Verlag 198/2(1996-02-01), 263-270 0032-0935 198:2<263 1996 198 425 https://doi.org/10.1007/BF00206252 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00206252 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Rawat Mamta Department of Plant Biology, Louisiana State University, 70803, Baton Rouge, LA, USA aut NATIONALLICENCE 700 1- Henk Margaret Department of Microbiology, Louisiana State University, 70803, Baton Rouge, LA, USA aut NATIONALLICENCE 700 1- Lavigne Lara Department of Biochemistry, Louisiana State University, 70803, Baton Rouge, LA, USA aut NATIONALLICENCE 700 1- Moroney James Department of Plant Biology, Louisiana State University, 70803, Baton Rouge, LA, USA aut NATIONALLICENCE 773 0- Planta Springer-Verlag 198/2(1996-02-01), 263-270 0032-0935 198:2<263 1996 198 425 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer