NDLI: ThnY Is a Ferredoxin Reductase-like Iron-Sulfur Flavoprotein That Has Evolved to Function as a Regulator of Tetralin Biodegradation Gene Expression*

Content Provider	PubMed Central
Author	García, Laura Ledesma Elena, Rivas-marín Floriano, Belén Bernhardt, Rita Ewen, Kerstin Maria Francisca, Reyes-ramírez Santero, Eduardo
Abstract	Previous genetic studies in Sphingomonas macrogolitabida strain TFA have established that expression of genes involved in tetralin biodegradation (thn genes) requires the function of the LysR type activator ThnR and also ThnY. Sequence comparison indicated that ThnY is homologous to bacterial oxygenase-coupled NAD(P)H-dependent ferredoxin reductases. However, ThnY showed substitutions in highly conserved positions of the pyridine nucleotide binding domain of these ferredoxin reductases. ThnY expression is co-regulated with all other genes required for tetralin biodegradation, and presumably thnY is part of the thnCA3A4RY operon. ThnY has been purified, and its biochemical and functional properties were characterized. ThnY was found to be a monomeric orange-brown iron-sulfur flavoprotein (estimated mass of 37,000 Da) containing one non-covalently attached flavin adenine dinucleotide and one plant type ferredoxin 2Fe-2S cluster. It can be efficiently reduced by dithionite, but reduction by pyridine nucleotides was very poor. Consistently, ThnY-dependent reduction of cytochrome c, ferricyanide, or 2,6-dichlorophenolindophenol using NAD(P)H as the electron donor was undetectable or very weak. The addition of ThnY to electrophoretic mobility shift assays containing ThnR and a probe bearing two thn divergent promoters resulted in a 3-fold increase in protein-DNA complex formation affinity, which indicates that ThnY directly promotes thn transcription activation by ThnR.
Related Links	http://dx.doi.org/10.1074/jbc.m110.184648
Ending Page	1718
Page Count	10
Starting Page	1709
File Format	PDF
ISSN	00219258
e-ISSN	1083351X
Journal	The Journal of Biological Chemistry
Issue Number	3
Volume Number	286
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2011-01-21
Access Restriction	Open
Rights Holder	American Society for Biochemistry and Molecular Biology
Subject Keyword	Cell Biology Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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

ThnY is a ferredoxin reductase-like iron-sulfur flavoprotein that has evolved to function as a regulator of tetralin biodegradation gene expression.

ThnY Is a Ferredoxin Reductase-like Iron-Sulfur Flavoprotein That Has Evolved to Function as a Regulator of Tetralin Biodegradation Gene Expression

The Ferredoxin ThnA3 Negatively Regulates Tetralin Biodegradation Gene Expression via ThnY, a Ferredoxin Reductase That Functions as a Regulator of the Catabolic Pathway

Ferredoxin-dependent Redox System of a Thermoacidophilic Archaeon, Sulfolobus sp. Strain 7 PURIFICATION AND CHARACTERIZATION OF A NOVEL REDUCED FERREDOXIN-REOXIDIZING IRON-SULFUR FLAVOPROTEIN

Crystallographic characterization of phthalate oxygenase reductase, an iron-sulfur flavoprotein from Pseudomonas cepacia.

Identification of the iron-sulfur center of spinach ferredoxin-nitrite reductase as a tetranuclear center, and preliminary EPR studies of mechanism.

Purification and properties of 5,10-methylenetetrahydrofolate reductase, an iron-sulfur flavoprotein from Clostridium formicoaceticum.

Structure–function studies on the complex iron–sulfur flavoprotein glutamate synthase: the key enzyme of ammonia assimilation

Structural prototypes for an extended family of flavoprotein reductases: comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin.

ThnY Is a Ferredoxin Reductase-like Iron-Sulfur Flavoprotein That Has Evolved to Function as a Regulator of Tetralin Biodegradation Gene Expression*

Similar Documents

ThnY is a ferredoxin reductase-like iron-sulfur flavoprotein that has evolved to function as a regulator of tetralin biodegradation gene expression.

ThnY Is a Ferredoxin Reductase-like Iron-Sulfur Flavoprotein That Has Evolved to Function as a Regulator of Tetralin Biodegradation Gene Expression

The Ferredoxin ThnA3 Negatively Regulates Tetralin Biodegradation Gene Expression via ThnY, a Ferredoxin Reductase That Functions as a Regulator of the Catabolic Pathway

Ferredoxin-dependent Redox System of a Thermoacidophilic Archaeon, Sulfolobus sp. Strain 7 PURIFICATION AND CHARACTERIZATION OF A NOVEL REDUCED FERREDOXIN-REOXIDIZING IRON-SULFUR FLAVOPROTEIN

Crystallographic characterization of phthalate oxygenase reductase, an iron-sulfur flavoprotein from Pseudomonas cepacia.

Identification of the iron-sulfur center of spinach ferredoxin-nitrite reductase as a tetranuclear center, and preliminary EPR studies of mechanism.

Purification and properties of 5,10-methylenetetrahydrofolate reductase, an iron-sulfur flavoprotein from Clostridium formicoaceticum.

Structure–function studies on the complex iron–sulfur flavoprotein glutamate synthase: the key enzyme of ammonia assimilation

Structural prototypes for an extended family of flavoprotein reductases: comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin.

ThnY Is a Ferredoxin Reductase-like Iron-Sulfur Flavoprotein That Has Evolved to Function as a Regulator of Tetralin Biodegradation Gene Expression*