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ID 17246
file
creator
Shintaku, Koki
Yonekawa, Yuki
Takatsu, Nariaki
Yamada, Hiroshi
Hamada, Yoshiyuki
Hirota, Hiroshi
Michibata, Hitoshi
subject
vanadium
ascidian
metal-binding protein
protein-protein interaction
NDC
Biology
abstract
Several species of ascidians, the so-called tunicates, accumulate extremely high levels of vanadium ions in their blood cells. We previously identified a family of vanadium-binding proteins, named Vanabins, from blood cells and blood plasma of a vanadium-rich ascidian, Ascidia sydneiensis samea. The 3-dimensional structure of Vanabin2, the predominant vanadium-binding protein in blood cells, has been revealed, and the vanadium-binding properties of Vanabin2 have been studied in detail. Here, we used Far Western blotting to identify a novel protein that interacts with Vanabin2 from a blood cell cDNA library. The protein, named Vanabin-interacting protein 1 (VIP1), was localized in the cytoplasm of signet ring cells and giant cells. Using a two-hybrid method, we revealed that VIP1 interacted with Vanabins 1, 2, 3, and 4 but not with Vanabin P. The N-terminal domain of VIP1 was shown to be important for the interaction. Further, Vanabin1 was found to interact with all of the other Vanabins. These results suggest that VIP1 and Vanabin1 act as metal chaperones or target proteins in vanadocytes.
journal title
Biochimica et Biophysica Acta - General Subjects
volume
Volume 1770
issue
Issue 6
start page
951
end page
957
date of issued
2007-06
publisher
Elsevier B.V.
issn
0304-4165
ncid
publisher doi
pubmed id
language
eng
nii type
Journal Article
HU type
Journal Articles
DCMI type
text
format
application/pdf
text version
author
rights
Copyright (c) 2007 Elsevier B.V.
relation is version of URL
http://dx.doi.org/10.1016/j.bbagen.2007.02.003
department
Graduate School of Science