Four signature motifs define the first class of structurally related large coiled-coil proteins in plants.
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Date
2002-04-09
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BioMed Central
Abstract
Background: Animal and yeast proteins containing long coiled-coil domains are involved in
attaching other proteins to the large, solid-state components of the cell. One subgroup of long
coiled-coil proteins are the nuclear lamins, which are involved in attaching chromatin to the nuclear
envelope and have recently been implicated in inherited human diseases. In contrast to other
eukaryotes, long coiled-coil proteins have been barely investigated in plants.
Results: We have searched the completed Arabidopsis genome and have identified a family of
structurally related long coiled-coil proteins. Filament-like plant proteins (FPP) were identified by
sequence similarity to a tomato cDNA that encodes a coiled-coil protein which interacts with the
nuclear envelope-associated protein, MAF1. The FPP family is defined by four novel unique
sequence motifs and by two clusters of long coiled-coil domains separated by a non-coiled-coil
linker. All family members are expressed in a variety of Arabidopsis tissues. A homolog sharing the
structural features was identified in the monocot rice, indicating conservation among angiosperms.
Conclusion: Except for myosins, this is the first characterization of a family of long coiled-coil
proteins in plants. The tomato homolog of the FPP family binds in a yeast two-hybrid assay to a
nuclear envelope-associated protein. This might suggest that FPP family members function in
nuclear envelope biology. Because the full Arabidopsis genome does not appear to contain genes
for lamins, it is of interest to investigate other long coiled-coil proteins, which might functionally
replace lamins in the plant kingdom.
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Frank Gindullis et al, "Four signature motifs define the first class of structurally related large coiled-coil proteins in plants," BMC Genomic 3 (2002), doi:10.1186/1471-2164-3-9, http://www.biomedcentral.com/1471-2164/3/9