NDLI: A major integral protein of the plant plasma membrane binds flavin

Content Provider	Springer Nature Link
Author	Lorenz, Astrid Kaldenhoff, Ralf Hertel, Rainer
Copyright Year	2003
Abstract	Abundant flavin binding sites have been found in membranes of plants and fungi. With flavin mononucleotide-agarose affinity columns, riboflavin-binding activity from microsomes of Cucurbita pepo L. hypocotyls was purified and identified as a specific PIP1-homologous protein of the aquaporin family. Sequences such as gi\|2149955 in Phaseolus vulgaris, PIP1b of Arabidopsis thaliana, and NtAQP1 of tobacco are closely related. The identification as a riboflavin-binding protein was confirmed by binding tests with an extract of Escherichia coli cells expressing the tobacco NtAQP1 as well as leaves of transgenic tobacco plants that overexpress NtAQP1 or were inhibited in PIP1 expression by antisense constructs. When binding was assayed in the presence of dithionite, the reduced flavin formed a relatively stable association with the protein. Upon dilution under oxidizing conditions, the adduct was resolved, and free flavin reappeared with a half time of about 30 min. Such an association can also be induced photochemically, with oxidized flavin by blue light at 450 nm, in the presence of an electron donor. Several criteria, localization in the plasma membrane, high abundance, affinity to roseoflavin, and photochemistry, argue for a role of the riboflavin-binding protein PIP1 as a photoreceptor.
Starting Page	19
Ending Page	30
Page Count	12
File Format	PDF
ISSN	0033183X
Journal	Protoplasma
Volume Number	221
Issue Number	1-2
e-ISSN	16156102
Language	English
Publisher	Springer-Verlag
Publisher Date	2003-05-01
Publisher Place	Wien
Access Restriction	One Nation One Subscription (ONOS)
Content Type	Text
Resource Type	Article
Subject	Cell Biology Plant Science Medicine

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