Chlamydomonas reinhardtii produces a profilin with unusual biochemical properties.

作者: Bjørn K. Drobak , David R. Kovar , Christopher J. Staiger , Winfield S. Sale , Pinfen Yang

DOI: 10.1242/JCS.114.23.4293

关键词:

摘要: We report the characterization of a profilin orthologue from Chlamydomonas reinhardtii. CrPRF, probably only isoform, is present in both cell body and flagella. Examination vegetative gametic cells by immunofluorescence microscopy using multiple fixation procedures also revealed enrichment CrPRF at anterior near base flagella fertilization tubule mating type plus gametes. Purified, recombinant binds to actin with Kd value ∼10–7 displaces nuclei live ‘nuclear displacement’ assay, consistent profilin’s ability bind G-actin vivo. However, when compared other isoforms, has relatively low affinity for poly-L-proline phosphatidylinositol (4,5) bisphosphate micelles. Furthermore, surprisingly, inhibits exchange adenine nucleotide on manner similar human ADF or DNase I. Thus, we postulate that primary role sequester Chlamydomonas. The unusual biochemical properties offer new opportunity distinguish specific functions isoforms.

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