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Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones.

Thaw, Paul and Baxter, Nicola J. and Hounslow, Andrea M. and Price, Clive and Waltho, Jonathan P. and Craven, C. Jeremy (2001) Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones. Nature Structural and Molecular Biology, 8 (8). pp. 701-704. ISSN 1072-8368

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Abstract

The translationally controlled tumor-associated proteins (TCTPs) are a highly conserved and abundantly expressed family of eukaryotic proteins that are implicated in both cell growth and the human acute allergic response but whose intracellular biochemical function has remained elusive. We report here the solution structure of the TCTP from Schizosaccharomyces pombe, which, on the basis of sequence homology, defines the fold of the entire family. We show that TCTPs form a structural superfamily with the Mss4/Dss4 family of proteins, which bind to the GDP/GTP free form of Rab proteins (members of the Ras superfamily) and have been termed guanine nucleotide-free chaperones (GFCs). Mss4 also acts as a relatively inefficient guanine nucleotide exchange factor (GEF). We further show that the Rab protein binding site on Mss4 coincides with the region of highest sequence conservation in the TCTP family. This is the first link to any other family of proteins that has been established for the TCTP family and suggests the presence of a GFC/GEF at extremely high abundance in eukaryotic cells.

Item Type: Article
Journal or Publication Title: Nature Structural and Molecular Biology
Subjects: Q Science > QH Natural history > QH301 Biology
Departments: Faculty of Health and Medicine > Biomedical & Life Sciences
ID Code: 9312
Deposited By: Dr Clive Price
Deposited On: 04 Jun 2008 11:30
Refereed?: Yes
Published?: Published
Last Modified: 26 Jul 2012 18:35
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/9312

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