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PMID: 3149301 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The molecular topography of phytochrome: chromophore and apoprotein.

Journal of photochemistry and photobiology. B, Biology ·Vol. 2 ·No. 1 ·1988-07-00 ·Pages 43-57

Song PS

Abstract

Phytochrome serves as the photochromic receptor for a number of morphogenic and developmental responses to red light in higher plants. The photoreversible phototransformation of 124 kDa oat phytochrome involves several structural changes in the chromophore and the apoprotein, including a configurational/conformational isomerization and secondary/tertiary structural changes respectively. For example, there appears to be a specific interaction between the chromophore and the amino terminus segment in the Pfr form of phytochrome, which results in a photoreversible peptide folding of the amino terminus peptide chain. Other structural changes also accompany the phototransformation, as has been probed by peptide mapping, phosphorylation, and monoclonal antibodies.

MeSH Terms
Amino Acid Sequence Apoproteins/metabolism Edible Grain Light Molecular Sequence Data Peptide Mapping Phytochrome/metabolism,radiation effects Plant Proteins/metabolism Plants/metabolism Protein Conformation
Chemicals
Apoproteins Plant Proteins Phytochrome
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Song P S
Department of Chemistry, School of Biological Sciences, University of Nebraska, Lincoln 68588-0304.
Article Info
Journal
Journal of photochemistry and photobiology. B, Biology
Abbr.
J Photochem Photobiol B
ISSN
1011-1344
Published
1988-07-00
Pages
43-57
Language
English
Region
Switzerland
NLM ID
8804966
Subset
IM
Grants
NIGMS NIH HHS · GM-36956 · United States
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