Tw. Mcnellis et al., GENETIC AND MOLECULAR ANALYSIS OF AN ALLELIC SERIES OF COP1 MUTANTS SUGGESTS FUNCTIONAL ROLES FOR THE MULTIPLE PROTEIN DOMAINS, The Plant cell, 6(4), 1994, pp. 487-500
The Arabidopsis protein COP1, encoded by the CONSTITUTIVE PHOTOMORPHOG
ENIC 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 f
ar-red treatment, and ratio of red/far-red light. The COP1 protein con
tains three recognizable structural domains: starting from the N termi
nus, they are the zinc binding motif, the putative coiled-coil region,
and the domain with multiple WD-40 repeats homologous to the P subuni
t of trimeric G-proteins (G(beta)) To understand the functional implic
ations of these structural motifs, 17 recessive mutations of the COP1
gene have been isolated based on their constitutive photomorphogenic s
eedling development in darkness. These mutations define three phenotyp
ic 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 prot
ein 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 s
tretches between the putative coiled-coil and G(beta)-protein homology
domains strongly compromised COP1 function. However, a mutation resul
ting in a COP1 protein with only the N-terminal 282 amino acids, inclu
ding both the zinc binding and the coiled-coil domains, produced a wea
k 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.