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Characterization of self-assembly of Euplotes octocarinatus centrin

Paper ID Volume ID Publish Year Pages File Format Full-Text
31113 44547 2009 7 PDF Available
Title
Characterization of self-assembly of Euplotes octocarinatus centrin
Abstract

Centrin, an EF-hand calcium-binding protein with high homology to calmodulin (CaM), is an essential component for microtubule-organizing center (MTOC) in organisms ranging from algae and yeast to human. It plays an important structural role by contributing to the formation of Ca2+-sensitive contractile filaments and some super-molecular assemblies. Previous work suggests that the N-terminal domain of centrin especially its first 20-residue fragment, is required for the self-assembly of protein. Native polyacrylamide gel electrophoresis (native-PAGE), pull-down assay, fluorescence resonance light scattering (RLS) and yeast two-hybrid assay indicate that the C-terminal domain of Euplotes octocarinatus centrin (EoCen) also contributes to the centrin self-assembly besides its N-terminal domain in vivo and in vitro. On the basis of our results, a self-assembly mode of centrin, which is C-to-C as well as N-to-N (between C- and C-terminal domains as well as between N- and N-terminal domains), is put forward providing maybe some insights into the molecular mechanism of centrin functions in the cell.

Keywords
MTOC, microtubule-organizing center; CRC, Chlamydomonas reinhardtii caltractin; EoCen, Euplotes octocarinatus centrin; N-EoCen, N-terminal domain of Euplotes octocarinatus centrin; C-EoCen, C-terminal domain of Euplotes octocarinatus centrin; HsCen1, huma
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Characterization of self-assembly of Euplotes octocarinatus centrin
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 95, Issue 1, 2 April 2009, Pages 26–32
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Price was $35.95
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