Purification and Reconstitution of PYP-Phytochrome with Biliverdin and 4-Hydroxycinnamic Acid.

Purification and Reconstitution of PYP-Phytochrome with Biliverdin and 4-Hydroxycinnamic Acid. Research Abstract Details 

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Purification and Reconstitution of PYP-Phytochrome with Biliverdin and 4-Hydroxycinnamic Acid. Abstract Text:

Young-Ho Chung,Shinji Masuda,Carl E Bauer,

PYP-phytochrome (Ppr) is a unique photoreceptor that contains a blue light-absorbing photoactive yellow protein (PYP) domain, a red light-absorbing phytochrome domain, and a histidine kinase domain. This chapter describes overexpression of Ppr in a strain of Escherichia coli that allows covalent attachment of substoichiometric amounts of biliverdin in vivo. Ppr is then fully reconstituted with biliverdin, followed by attachment of 4-hydroxycinnamic acid (p-coumaric acid), in vitro. Holo-Ppr with both chromophores is then isolated via an affinity tag and quantified for chromophore attachment by analysis of the absorption spectrum for biliverdin and 4-hydroxycinnamic acid. We also provide conditions for measuring autophosphorylation of Ppr.

Purification and Reconstitution of PYP-Phytochrome with Biliverdin and 4-Hydroxycinnamic Acid. Publishing Authors By Initials

YH Chung,S Masuda,CE Bauer,

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Purification and Reconstitution of PYP-Phytochrome with Biliverdin and 4-Hydroxycinnamic Acid. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Methods in enzymology

VOLUME: 422

Page Numbers: 184-9

Journal Abbreviation: Meth. Enzymol.

ISSN: 0076-6879

DAY: 13

MONTH: 07

YEAR: 2007

Purification and Reconstitution of PYP-Phytochrome with Biliverdin and 4-Hydroxycinnamic Acid. Information

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LANGUAGE: eng

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