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Four signature motifs define the first class of structurally related large coiled-coil proteins in plants.

Gindullis F, Rose A, Patel S, Meier I - BMC Genomics (2002)

Bottom Line: 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 tomato homolog of the FPP family binds in a yeast two-hybrid assay to a nuclear envelope-associated protein.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.

View Article: PubMed Central - HTML - PubMed

Affiliation: CellTec Biotechnologie GmbH, Frohmestrasse 110, D-22459 Hamburg, Germany. frank.gindullis@celltec.de

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.

No MeSH data available.


Related in: MedlinePlus

Phylogenetic tree derived from a CLUSTAL analysis of the full ORF sequences of Arabidopsis coiled-coil proteins. The seven AtFPP sequences (boxed) were aligned together with 35 additional Arabidopsis coiled-coil proteins that had been annotated as "myosin-like". The length of each pair of branches measures the distance between sequences. Units indicate the number of computed residue substitution events. Dotted lines have no unit length and were included for alignment purposes. ORFs were identified by their TAIR gene names, accessible through .
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Figure 5: Phylogenetic tree derived from a CLUSTAL analysis of the full ORF sequences of Arabidopsis coiled-coil proteins. The seven AtFPP sequences (boxed) were aligned together with 35 additional Arabidopsis coiled-coil proteins that had been annotated as "myosin-like". The length of each pair of branches measures the distance between sequences. Units indicate the number of computed residue substitution events. Dotted lines have no unit length and were included for alignment purposes. ORFs were identified by their TAIR gene names, accessible through .

Mentions: The 35 new sequences were aligned with the seven AtFPP sequences in a CLUSTAL analysis. Fig. 5 shows the results represented as a phylogenetic tree. The AtFPP family clearly forms a family of sequences separate from the other coiled-coil proteins (boxed in Fig. 5). The three "short" AtFPPs, AtFPP1, AtFPP2, and AtFPP3 form a sub-family, as do the four "long" AtFPPs AtFPP4, AtFPP5, AtFPP6, and AtFPP7 (see Fig. 3). Interestingly, the two most closely related AtFPP genes, AtFPP1 and AtFPP2 are located in comparable positions on two duplicated segments of chromosome 1, indicating that they might be derived from a recent duplication event.


Four signature motifs define the first class of structurally related large coiled-coil proteins in plants.

Gindullis F, Rose A, Patel S, Meier I - BMC Genomics (2002)

Phylogenetic tree derived from a CLUSTAL analysis of the full ORF sequences of Arabidopsis coiled-coil proteins. The seven AtFPP sequences (boxed) were aligned together with 35 additional Arabidopsis coiled-coil proteins that had been annotated as "myosin-like". The length of each pair of branches measures the distance between sequences. Units indicate the number of computed residue substitution events. Dotted lines have no unit length and were included for alignment purposes. ORFs were identified by their TAIR gene names, accessible through .
© Copyright Policy
Related In: Results  -  Collection

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getmorefigures.php?uid=PMC102765&req=5

Figure 5: Phylogenetic tree derived from a CLUSTAL analysis of the full ORF sequences of Arabidopsis coiled-coil proteins. The seven AtFPP sequences (boxed) were aligned together with 35 additional Arabidopsis coiled-coil proteins that had been annotated as "myosin-like". The length of each pair of branches measures the distance between sequences. Units indicate the number of computed residue substitution events. Dotted lines have no unit length and were included for alignment purposes. ORFs were identified by their TAIR gene names, accessible through .
Mentions: The 35 new sequences were aligned with the seven AtFPP sequences in a CLUSTAL analysis. Fig. 5 shows the results represented as a phylogenetic tree. The AtFPP family clearly forms a family of sequences separate from the other coiled-coil proteins (boxed in Fig. 5). The three "short" AtFPPs, AtFPP1, AtFPP2, and AtFPP3 form a sub-family, as do the four "long" AtFPPs AtFPP4, AtFPP5, AtFPP6, and AtFPP7 (see Fig. 3). Interestingly, the two most closely related AtFPP genes, AtFPP1 and AtFPP2 are located in comparable positions on two duplicated segments of chromosome 1, indicating that they might be derived from a recent duplication event.

Bottom Line: 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 tomato homolog of the FPP family binds in a yeast two-hybrid assay to a nuclear envelope-associated protein.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.

View Article: PubMed Central - HTML - PubMed

Affiliation: CellTec Biotechnologie GmbH, Frohmestrasse 110, D-22459 Hamburg, Germany. frank.gindullis@celltec.de

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.

No MeSH data available.


Related in: MedlinePlus