NDLI: Light activation of the LOV protein Vivid generates a rapidly exchanging dimer† ‡

Content Provider	PubMed Central
Author	Zoltowski, Brian D. Crane, Brian R.
Abstract	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 β-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-to-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 Neurospora crassa, and indicate that LOV:LOV homo or hetero dimerization may be a mechanism for regulating light-activated gene expression.
Related Links	http://dx.doi.org/10.1021/bi8007017
Ending Page	7019
Page Count	8
Starting Page	7012
File Format	PDF
ISSN	00062960
e-ISSN	15204995
Journal	Biochemistry
Issue Number	27
Volume Number	47
Language	English
Publisher Date	2008-07-01
Access Restriction	Open
Subject Keyword	Biochemistry Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biochemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The PAS/LOV protein VIVID supports a rapidly dampened daytime oscillator that facilitates entrainment of the Neurospora circadian clock

Structure of a light-activated LOV protein dimer that regulates transcription in Neurospora crassa

Light-induced structural changes in a short light, oxygen, voltage (LOV) protein revealed by molecular dynamics simulations—implications for the understanding of LOV photoactivation

The PAS/LOV protein VIVID controls temperature compensation of circadian clock phase and development in Neurospora crassa

Revealing Hidden Conformational Space of LOV Protein VIVID Through Rigid Residue Scan Simulations

Light-induced structural changes in a short light, oxygen, voltage (LOV) protein revealed by molecular dynamics simulations—implications for the understanding of LOV photoactivation

Blue light diminishes interaction of PAS/LOV proteins, putative blue light receptors in Arabidopsis thaliana, with their interacting partners

Examination of the hydrophobicity of the LOV (Light-Oxygen-Voltage) protein active site, using computational chemistry and Raman spectroscopy

Light-Induced Subunit Dissociation by a LOV domain Photoreceptor from Rhodobacter sphaeroides

Light activation of the LOV protein Vivid generates a rapidly exchanging dimer† ‡

Similar Documents

The PAS/LOV protein VIVID supports a rapidly dampened daytime oscillator that facilitates entrainment of the Neurospora circadian clock

Structure of a light-activated LOV protein dimer that regulates transcription in Neurospora crassa

Light-induced structural changes in a short light, oxygen, voltage (LOV) protein revealed by molecular dynamics simulations—implications for the understanding of LOV photoactivation

The PAS/LOV protein VIVID controls temperature compensation of circadian clock phase and development in Neurospora crassa

Revealing Hidden Conformational Space of LOV Protein VIVID Through Rigid Residue Scan Simulations

Light-induced structural changes in a short light, oxygen, voltage (LOV) protein revealed by molecular dynamics simulations—implications for the understanding of LOV photoactivation

Blue light diminishes interaction of PAS/LOV proteins, putative blue light receptors in Arabidopsis thaliana, with their interacting partners

Examination of the hydrophobicity of the LOV (Light-Oxygen-Voltage) protein active site, using computational chemistry and Raman spectroscopy

Light-Induced Subunit Dissociation by a LOV domain Photoreceptor from Rhodobacter sphaeroides

Light activation of the LOV protein Vivid generates a rapidly exchanging dimer† ‡