Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.M112.379859
Title: NMR structure of Carcinoscorpius rotundicauda thioredoxin-related protein 16 and its role in regulating transcription factor NF-κB activity
Authors: Giri, P.K.
Jing-Song, F. 
Shanmugam, M.K. 
Ding, J.L. 
Sethi, G.
Swaminathan, K. 
Sivaraman, J. 
Issue Date: 24-Aug-2012
Citation: Giri, P.K., Jing-Song, F., Shanmugam, M.K., Ding, J.L., Sethi, G., Swaminathan, K., Sivaraman, J. (2012-08-24). NMR structure of Carcinoscorpius rotundicauda thioredoxin-related protein 16 and its role in regulating transcription factor NF-κB activity. Journal of Biological Chemistry 287 (35) : 29417-29428. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.M112.379859
Related Datasets: 10635/137407
Abstract: Thioredoxins (Trxs), which play a key role in maintaining a redox environment in the cell, are found in almost all organisms. Trxs act as potential reducing agents of disulfide bonds and contain two vicinal cysteines in a CXXC motif at the active site. Trx is also known to activate the DNA binding activity of NF-κB, an important transcription factor. Previously, Trx-related protein 16 from Carcinoscorpius rotundicauda (Cr-TRP16), a 16-kDa Trx-like protein that contains a WCPPC motif, was reported. Here we present the NMR structure of the reduced form of Cr-TRP16, along with its regulation of NF-κB activity. Unlike other 16-kDa Trx-like proteins, Cr-TRP16 contains an additional Cys residue (Cys-15, at the N terminus), through which it forms a homodimer. Moreover, we have explored the molecular basis of Cr-TRP16-mediated activation of NF-κB and showed that Cr-TRP16 exists as a dimer under physiological conditions, and only the dimeric form binds to NF-κB and enhances its DNA binding activity by directly reducing the cysteines in the DNA-binding motif of NF-κB. The C15S mutant of Cr-TRP16 was unable to dimerize and hence does not bind to NF-κB. Based on our finding and combined with the literature, we propose a model of how Cr-TRP16 is likely to bind to NF-κB. These findings elucidate the molecular mechanism by which NF-κB activation is regulated through Cr-TRP16. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.
Source Title: Journal of Biological Chemistry
URI: http://scholarbank.nus.edu.sg/handle/10635/109487
ISSN: 00219258
DOI: 10.1074/jbc.M112.379859
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

3
checked on Jul 9, 2019

WEB OF SCIENCETM
Citations

4
checked on Jul 9, 2019

Page view(s)

45
checked on Jun 21, 2019

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.