Open AccessAdenosine 3′:5′-Cyclic Monophosphate in Chlamydomonas reinhardtii: Isolation and Characterization
Author(s) -
Nikolaus Amrhein,
Philip Filner
Publication year - 1973
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.70.4.1099
Subject(s) - chlamydomonas reinhardtii , adenosine , chlamydomonas , biochemistry , chemistry , isolation (microbiology) , adenosine monophosphate , adenosine triphosphate , biology , gene , bioinformatics , mutant
Chlamydomonas reinhardtii contains a factor that can replace adenosine 3′:5′-cyclic monophosphate (cAMP) in the stimulation of rabbit-muscle protein kinase. The factor cochromatographs and coelectrophoreses with authentic cAMP, and is inactivated by beef heart cyclic nucleotide phosphodiesterase. WhenC. reinhardtii is exposed to aminophylline (theophylline2 ethylenediamine), the concentration of the factor in the cells increases within 1 hr, from about 25 pmol of cAMP equivalents per g dry weight to more than 250 pmol. Cyclic nucleotide phosphodiesterase activity is present in crude extract ofC. reinhardtii and is inhibited by theophylline. We conclude that cAMP occurs inC. reinhardtii and that the endogenous concentration is governed at least in part by a theophylline-sensitive cyclic nucleotide phosphodiesterase. These findings provide a sound basis for attributing the effects of methylxanthines on flagellar function and regeneration inC. reinhardtii to the resultant elevation of endogenous cAMP.