Blue protein with red fluorescence.

Autor: Ghosh S; National Center for Biological Sciences, Tata Institute of Fundamental Research, Bangalore, India 560065., Yu CL; Department of Microbiology, University of Iowa, Iowa City, IA 52242., Ferraro DJ; Department of Biochemistry, University of Iowa, Iowa City, IA 52242., Sudha S; Institute for Stem Cell Biology and Regenerative Medicine, Bangalore, India 560065., Pal SK; Department of Chemical, Biological & Macromolecular Sciences, S.N. Bose National Centre for Basic Sciences, Salt Lake, Kolkata 700 098, India., Schaefer WF; Department of Biological Sciences, University of Wisconsin, Washington County, WI 53095., Gibson DT; Department of Microbiology, University of Iowa, Iowa City, IA 52242., Ramaswamy S; Department of Biochemistry, University of Iowa, Iowa City, IA 52242; Institute for Stem Cell Biology and Regenerative Medicine, Bangalore, India 560065; ramas@instem.res.in.
Jazyk: angličtina
Zdroj: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2016 Oct 11; Vol. 113 (41), pp. 11513-11518. Date of Electronic Publication: 2016 Sep 29.
DOI: 10.1073/pnas.1525622113
Abstrakt: The walleye (Sander vitreus) is a golden yellow fish that inhabits the Northern American lakes. The recent sightings of the blue walleye and the correlation of its sighting to possible increased UV radiation have been proposed earlier. The underlying molecular basis of its adaptation to increased UV radiation is the presence of a protein (Sandercyanin)-ligand complex in the mucus of walleyes. Degradation of heme by UV radiation results in the formation of Biliverdin IXα (BLA), the chromophore bound to Sandercyanin. We show that Sandercyanin is a monomeric protein that forms stable homotetramers on addition of BLA to the protein. A structure of the Sandercyanin-BLA complex, purified from the fish mucus, reveals a glycosylated protein with a lipocalin fold. This protein-ligand complex absorbs light in the UV region (λ max of 375 nm) and upon excitation at this wavelength emits in the red region (λ max of 675 nm). Unlike all other known biliverdin-bound fluorescent proteins, the chromophore is noncovalently bound to the protein. We provide here a molecular rationale for the observed spectral properties of Sandercyanin.
Competing Interests: The authors declare no conflict of interest.
Databáze: MEDLINE