Molecular and Cellular Biochemistry

, Volume 230, Issue 1, pp 149–158

Guanylyl cyclases in unicellular organisms

  • Jürgen U. Linder
  • Joachim E. Schultz

DOI: 10.1023/A:1014200325422

Cite this article as:
Linder, J.U. & Schultz, J.E. Mol Cell Biochem (2002) 230: 149. doi:10.1023/A:1014200325422


Guanylyl cyclases in eukaryotic unicells were biochemically investigated in the ciliates Paramecium and Tetrahymena, in the malaria parasite Plasmodium and in the ameboid Dictyostelium. In ciliates guanylyl cyclase activity is calcium-regulated suggesting a structural kinship to similarly regulated membrane-bound guanylyl cyclases in vertebrates. Yet, cloning of ciliate guanylyl cyclases revealed a novel combination of known modular building blocks. Two cyclase homology domains are inversely arranged in a topology of mammalian adenylyl cyclases, containing two cassettes of six transmembrane spans. In addition the protozoan guanylyl cyclases contain an N-terminal P-type ATPase-like domain. Sequence comparisons indicate a compromised ATPase function. The adopted novel function remains enigmatic to date. The topology of the guanylyl cyclase domain in all protozoans investigated is identical. A recently identified Dictyostelium guanylyl cyclase lacks the N-terminal P-type ATPase domain. The close functional relation of Paramecium guanylyl cyclases to mammalian adenylyl cyclases has been established by heterologous expression, respective point mutations and a series of active mammalian adenylyl cyclase/Paramecium guanylyl cyclase chimeras. The unique structure of protozoan guanylyl cyclases suggests that unexpectedly they do not share a common guanylyl cyclase ancestor with their vertebrate congeners but probably originated from an ancestral mammalian-type adenylyl cyclase.

guanylyl cyclase adenylyl cyclase Paramecium Plasmodium Tetrahymena Dictyostelium calcium calmodulin evolution chimera substrate specificity 

Copyright information

© Kluwer Academic Publishers 2002

Authors and Affiliations

  • Jürgen U. Linder
  • Joachim E. Schultz

There are no affiliations available

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