Partial characterization of a new isoenzyme of carbonic anhydrase isolated from Chlamydomonas reinhardtii.
A new isoenzyme of carbonic anhydrase has been isolated and purified from Chlamydomonas reinhardtii. This carbonic anhydrase is composed of two nonidentical subunits with apparent molecular masses of 39 and 4.5 kDa and is located in the periplasmic space. This is the second periplasmic carbonic anhydrase found in C. reinhardtii. Two genes, CAH1 and CAH2, which code for carbonic anhydrase, have been recently described by Fujiwara et al. (Fujiwara, S., Fukuzawa, H., Tachiki, A., and Miyachi, S. (1990) Proc. Natl. Acad, Sci. U.S.A. 87, 9779-9783). The CAH1 gene codes for a periplasmic carbonic anhydrase which is induced under low CO2 conditions and is well characterized. The carbonic anhydrase characterized in this report was isolated from a mutant that is unable to synthesize the CAH1 gene product. Amino acid sequencing demonstrates that this newly isolated carbonic anhydrase is the CAH2 gene product. This is the first report of another functional carbonic anhydrase in C. reinhardtii.
Rawat
M
M
Department of Botany, Louisiana State University, Baton Rouge 70803.
Moroney
J V
JV
D000595:Amino Acid Sequence; D015153:Blotting, Western; D002256:Carbonic Anhydrases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D002696:Chlamydomonas / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D007527:Isoenzymes / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data
D007527:Isoenzymes; D002256:Carbonic Anhydrases