Molecular determinant modulates thermal recovery kinetics and structural integrity of the bacterial BLUF photoreceptor. Issue 14 (12th June 2016)

• Record Type: Journal Article
• Authors: Tanwar, Meenakshi; Nahar, Smita; Gulati, Sahil; Veetil, Sindhu Kandoth; Kateriya, Suneel
• Is Part Of: FEBS letters. Volume 590:Issue 14(2016)
• Page Start: 2146
• Page End: 2157
• Publication Date: 2016-06-12
• Subjects: BLUF -- C terminus -- dark recovery kinetics -- photoreceptors -- Stenotrophomonas sp. SKA14; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12227
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : BLUF domains are flavin‐based photoreceptors which receive the blue light signal and are involved in the sensory transduction. We report a short BLUF photoreceptor (SnfB) in Stenotrophomonas sp . We have investigated photodynamic properties of C terminus truncated and several mutated SnfB proteins. Deletion of the extended C‐terminal residues alters the thermal recovery kinetics and also affects the integrity of the SnfB protein. Mutagenesis studies demonstrated that the conserved residues within and outside the flavin‐binding pocket also regulates the photocycle properties of the protein. These studies suggest that the C‐terminal residues outside the BLUF domain can tune the photodynamic properties of the BLUF protein. Abstract : Residues outside and within the flavin‐binding pocket modulates the recovery kinetics of SnfB. C terminus modulates the photodynamic properties of the SnfB protein. C terminus maintains the structure integrity of the SnfB protein. Truncation of the C terminus leads to oligomerization of the SnfB protein.