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COMPARISON OF THE PROTEIN CONFORMATIONS BETWEEN DIFFERENT FORMS (P r AND P fr ) OF NATIVE (124 kDa) AND DEGRADED (118/114 kDa) PHYTOCHROMES FROM Avena sativa *
Author(s) -
Vierstra Richard D.,
Quail Peter H.,
Hahn TaeRyong,
Song PillSoon
Publication year - 1987
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1987.tb05398.x
Subject(s) - phytochrome , avena , etiolation , chromophore , phytochrome a , biology , biochemistry , biophysics , chemistry , crystallography , botany , enzyme , photochemistry , red light , mutant , arabidopsis , gene
— Circular dichroic properties of native, 124 kDa phytochrome from etiolated Avena sativa seedlings have been examined and compared with those of degraded phytochrome (118/114 kDa). The CD spectrum of the P r form of 124 kDa phytochrome does not differ significantly in the visible region from that of 118/114 kDa P r . In contrast, the CD spectrum of the P fr form of 124 kDa phytochrome differs from that of the 118/114 kDa species in the far‐red, red and blue regions of the spectrum. This result confirms that the NH 2 ‐terminal polypeptide segment has a critical role in chromophore‐protein interaction in the P fr but not in the P r form. In the UV region, 124 kDa phytochrome exhibits a photoreversible difference between the CD spectra of P r and P fr , whereas no such difference is observed for 118/114 kDa preparations. These data suggest a possible photoreversible change in secondary structure of the 124 kDa phytochrome polypeptide that requires the presence of the 6/10 kDa NH 2 ‐terminal domain to occur.