Phototransformation of Pea Phytochrome A Induces an Increase in .alpha.-Helical Folding of the Apoprotein: Comparison with a Monocot Phytochrome A and CD Analysis by Different Methods
- 1 April 1994
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 33 (16) , 4918-4922
- https://doi.org/10.1021/bi00182a021
Abstract
The photoreversible conformational change associated with the Pr-->Pfr transformation of a dicot phytochrome A (Pisum sativum, pea) has been probed by circular dichroism (CD) studies. Three different CD analysis methods have been used to determine the secondary structure of pea phytochrome A in both Pr and Pfr forms. We have shown that the secondary structure of dicot pea phytochrome A is very similar to the structure of monocot oat phytochrome A which was determined earlier [Sommer & Song (1990) Biochemistry 29, 1943-1948]. As with oat phytochrome A, an increase in the alpha-helical folding of the apoprotein takes place when photochrome in the Pr form is phototransformed to the Pfr form. This conformational change might well be a general characteristic of all phytochrome A's.Keywords
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