Few substitutions affect the bioluminescence spectra of Phrixotrix (Coleoptera: Phengodidae) luciferases: a site-directed mutagenesis survey

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorViviani, Vadim R.
dc.creatorArnoldi, Frederico G.C.
dc.creatorOgawa, Florisbela T.
dc.creatorBrochetto-Braga, M.
dc.date2014-05-27T11:22:30Z
dc.date2016-10-25T18:24:00Z
dc.date2014-05-27T11:22:30Z
dc.date2016-10-25T18:24:00Z
dc.date2007-07-01
dc.date.accessioned2017-04-06T01:25:22Z
dc.date.available2017-04-06T01:25:22Z
dc.identifierLuminescence, v. 22, n. 4, p. 362-369, 2007.
dc.identifier1522-7235
dc.identifier1522-7243
dc.identifierhttp://hdl.handle.net/11449/69729
dc.identifierhttp://acervodigital.unesp.br/handle/11449/69729
dc.identifier10.1002/bio.972
dc.identifier2-s2.0-34548061218
dc.identifierhttp://dx.doi.org/10.1002/bio.972
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/890933
dc.descriptionPhrixotrix (railroad worm) luciferases produce bioluminescence in the green and red regions of the spectrum, depending on the location of the lanterns, and are the only luciferases naturally producing red bioluminescence. Comparison of the luciferase sequences showed a set of substitutions that could be involved in bioluminescence colour determination: (a) unique substitutions in the red luciferase replacing otherwise invariant residues; (b) conserved basic residues in the green-yellow emitting luciferases; and (c) an additional R353 residue in red-emitting luciferase (Viviani et al., 1999). To investigate whether these sites have a functional role in bioluminescence colour determination, we performed a site-directed mutagenesis. Natural substitutions in the region 220-344 and residues in the putative luciferin-binding site were also investigated. With the exception of the previously identified substitution of R215 and T226 (Viviani et al., 2002), which display dramatic red-shift effects on the spectrum of green-yellow-emitting luciferases, only a few substitutions had a moderate effect on the spectrum of the green-emitting luciferase. In contrast, no single substitution affected the spectrum of the red-emitting luciferase. The results suggest that the identity of the active site residues is not so critical for determining red bioluminescence in PxRE luciferase. Rather, the conformation assumed during the emitting step could be critical to set up proper interactions with excited oxyluciferin. Copyright ©2007 John Wiley & Sons, Ltd.
dc.languageeng
dc.relationLuminescence
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectBioluminescence
dc.subjectClick beetles
dc.subjectFireflies
dc.subjectLuciferases
dc.subjectPhrixotrix
dc.subjectRailroad worms
dc.subjectindole derivative
dc.subjectluciferase
dc.subjectoxyluciferin
dc.subjectphotoprotein
dc.subjectpyrazine derivative
dc.subjectunclassified drug
dc.subjectamino acid substitution
dc.subjectbinding site
dc.subjectchemistry
dc.subjectcolor
dc.subjectgenetics
dc.subjectluminescence
dc.subjectsite directed mutagenesis
dc.subjectspectroscopy
dc.subjectAmino Acid Substitution
dc.subjectBinding Sites
dc.subjectColor
dc.subjectIndoles
dc.subjectLuminescent Measurements
dc.subjectLuminescent Proteins
dc.subjectMutagenesis, Site-Directed
dc.subjectPyrazines
dc.subjectSpectrum Analysis
dc.subjectColeoptera
dc.subjectElateridae
dc.subjectLampyridae
dc.subjectPhengodidae
dc.titleFew substitutions affect the bioluminescence spectra of Phrixotrix (Coleoptera: Phengodidae) luciferases: a site-directed mutagenesis survey
dc.typeOtro


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