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THE PLANT CELL, Vol 6, Issue 4 487-500, Copyright © 1994 by American Society of Plant Biologists
Genetic and Molecular Analysis of an Allelic Series of cop1 Mutants Suggests Functional Roles for the Multiple Protein Domains
T. W. McNellis, A. G. von Arnim, T. Araki, Y. Komeda, S. Misera and X. W. Deng
Department of Biology, Yale University, New Haven, Connecticut 06520-8104
The Arabidopsis protein COP1, encoded by the CONSTITUTIVE PHOTOMORPHOGENIC
locus 1, is an essential regulatory molecule that plays a role in the
repression of photomorphogenic development in darkness and in the ability
of light-grown plants to respond to photoperiod, end-of-day far-red
treatment, and ratio of red/far-red light. The COP1 protein contains three
recognizable structural domains: starting from the N terminus, they are the
zinc binding motif, the putative coiled-coil region, and the domain with
multiple WD-40 repeats homologous to the [beta] subunit of trimeric
G-proteins (G[beta]). To understand the functional implications of these
structural motifs, 17 recessive mutations of the COP1 gene have been
isolated based on their constitutive photomorphogenic seedling development
in darkness. These mutations define three phenotypic classes: weak, strong,
and lethal. The mutations that fall into the lethal class are possible null
mutations of COP1. Molecular analysis of the nine mutant alleles that
accumulated mutated forms of COP1 protein revealed that disruption of the
G[beta]-protein homology domain or removal of the very C-terminal 56 amino
acids are both deleterious to COP1 function. In-frame deletions or
insertions of short amino acid stretches between the putative coiled-coil
and G[beta]-protein homology domains strongly compromised COP1 function.
However, a mutation resulting in a COP1 protein with only the N-terminal
282 amino acids, including both the zinc binding and the coiled-coil
domains, produced a weak phenotypic defect. These results indicated that
the N-terminal half of COP1 alone retains some activity and a disrupted
C-terminal domain masks this remaining activity.
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