Document Detail

Light-induced differences in conformational dynamics of the circadian clock regulator VIVID.
MedLine Citation:
PMID:  24189053     Owner:  NLM     Status:  Publisher    
The light-oxygen-voltage (LOV) domain protein VIVID (VVD) is a negative regulator of the circadian transcription factor White Collar Complex (WCC) and controls light response and photoadaptation in Neurospora. Blue light converts VIVID from the dark state into the light state (VVDL) with concomitant homodimerization. Upon return to low light conditions VVD very slowly reverts back into the monomeric dark state (VVDD). To better understand the nature of the conformational changes that are the basis for the light-dark switch in VVD, we used hydrogen exchange mass spectrometry (HX-MS) to probe solvent accessibility of backbone amide protons. Our data demonstrate that all structural elements of VVDD except for the N-cap region exchange according to the rare EX1 mechanism indicating a reversible unfolding with rather slow refolding rate. Interestingly, the unfolding halftimes of different elements were not identical but varied from 400 to 900s. VVDL also exchanges according to the EX1 mechanism, albeit with a halftime of 6h. Surprisingly, the dimerization interface showed very little protection suggesting a rapid dimer-monomer interconversion.
Chung-Tien Lee; Erik Malzahn; Michael Brunner; Matthias P Mayer
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-11-1
Journal Detail:
Title:  Journal of molecular biology     Volume:  -     ISSN:  1089-8638     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2013 Nov 
Date Detail:
Created Date:  2013-11-5     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
© 2013.
Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH-Alliance, Heidelberg, Germany.
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