pubmed-article:18553928 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18553928 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:18553928 | lifeskim:mentions | umls-concept:C0023693 | lld:lifeskim |
pubmed-article:18553928 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:18553928 | lifeskim:mentions | umls-concept:C1637379 | lld:lifeskim |
pubmed-article:18553928 | lifeskim:mentions | umls-concept:C0596448 | lld:lifeskim |
pubmed-article:18553928 | pubmed:issue | 27 | lld:pubmed |
pubmed-article:18553928 | pubmed:dateCreated | 2008-7-1 | lld:pubmed |
pubmed-article:18553928 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18553928 | pubmed:abstractText | The fungal photoreceptor Vivid (VVD) plays an important role in the adaptation of blue-light responses in Neurospora crassa. VVD, an FAD-binding LOV (light, oxygen, voltage) protein, couples light-induced cysteinyl adduct formation at the flavin ring to conformational changes in the N-terminal cap (Ncap) of the VVD PAS domain. Size-exclusion chromatography (SEC), equilibrium ultracentrifugation, and static and dynamic light scattering show that these conformational changes generate a rapidly exchanging VVD dimer, with an expanded hydrodynamic radius. A three-residue N-terminal beta-turn that assumes two different conformations in a crystal structure of a VVD C71V variant is essential for light-state dimerization. Residue substitutions at a critical hinge between the Ncap and PAS core can inhibit or enhance dimerization, whereas a Tyr to Trp substitution at the Ncap-PAS interface stabilizes the light-state dimer. Cross-linking through engineered disulfides indicates that the light-state dimer differs considerably from the dark-state dimer found in VVD crystal structures. These results verify the role of Ncap conformational changes in gating the photic response of N. crassa and indicate that LOV-LOV homo- or heterodimerization may be a mechanism for regulating light-activated gene expression. | lld:pubmed |
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pubmed-article:18553928 | pubmed:language | eng | lld:pubmed |
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pubmed-article:18553928 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:18553928 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18553928 | pubmed:month | Jul | lld:pubmed |
pubmed-article:18553928 | pubmed:issn | 1520-4995 | lld:pubmed |
pubmed-article:18553928 | pubmed:author | pubmed-author:CraneBrian... | lld:pubmed |
pubmed-article:18553928 | pubmed:author | pubmed-author:ZoltowskiBria... | lld:pubmed |
pubmed-article:18553928 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:18553928 | pubmed:day | 8 | lld:pubmed |
pubmed-article:18553928 | pubmed:volume | 47 | lld:pubmed |
pubmed-article:18553928 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18553928 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18553928 | pubmed:pagination | 7012-9 | lld:pubmed |
pubmed-article:18553928 | pubmed:dateRevised | 2011-8-1 | lld:pubmed |
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pubmed-article:18553928 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18553928 | pubmed:articleTitle | Light activation of the LOV protein vivid generates a rapidly exchanging dimer. | lld:pubmed |
pubmed-article:18553928 | pubmed:affiliation | Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA. | lld:pubmed |
pubmed-article:18553928 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18553928 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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