Limits...
Comparison of the receptor FGFRL1 from sea urchins and humans illustrates evolution of a zinc binding motif in the intracellular domain.

Zhuang L, Karotki AV, Bruecker P, Trueb B - BMC Biochem. (2009)

Bottom Line: FGFRL1, the gene for the fifth member of the fibroblast growth factor receptor (FGFR) family, is found in all vertebrates from fish to man and in the cephalochordate amphioxus.Since it does not occur in more distantly related invertebrates such as insects and nematodes, we have speculated that FGFRL1 might have evolved just before branching of the vertebrate lineage from the other invertebrates (Beyeler and Trueb, 2006).A comparison of the intracellular domain between sea urchin and human FGFRL1 provides interesting insights into the shaping of a novel zinc binding domain.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Clinical Research, University of Bern, 3010 Bern, Switzerland. lei.zhuang@dkf.unibe.ch

ABSTRACT

Background: FGFRL1, the gene for the fifth member of the fibroblast growth factor receptor (FGFR) family, is found in all vertebrates from fish to man and in the cephalochordate amphioxus. Since it does not occur in more distantly related invertebrates such as insects and nematodes, we have speculated that FGFRL1 might have evolved just before branching of the vertebrate lineage from the other invertebrates (Beyeler and Trueb, 2006).

Results: We identified the gene for FGFRL1 also in the sea urchin Strongylocentrotus purpuratus and cloned its mRNA. The deduced amino acid sequence shares 62% sequence similarity with the human protein and shows conservation of all disulfides and N-linked carbohydrate attachment sites. Similar to the human protein, the S. purpuratus protein contains a histidine-rich motif at the C-terminus, but this motif is much shorter than the human counterpart. To analyze the function of the novel motif, recombinant fusion proteins were prepared in a bacterial expression system. The human fusion protein bound to nickel and zinc affinity columns, whereas the sea urchin protein barely interacted with such columns. Direct determination of metal ions by atomic absorption revealed 2.6 mole zinc/mole protein for human FGFRL1 and 1.7 mole zinc/mole protein for sea urchin FGFRL1.

Conclusion: The FGFRL1 gene has evolved much earlier than previously assumed. A comparison of the intracellular domain between sea urchin and human FGFRL1 provides interesting insights into the shaping of a novel zinc binding domain.

Show MeSH

Related in: MedlinePlus

Phylogenetic analysis of the FGFRL1 sequences. An unrooted tree was built by the neighbour joining method. Bootstrap values from 1000 random replicates are indicated at the nodes. The length of the branches inversely correlates with the degree of similarity. Only the sequences from the extracellular domains without signal peptides and transmembrane domains were used.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC2806250&req=5

Figure 2: Phylogenetic analysis of the FGFRL1 sequences. An unrooted tree was built by the neighbour joining method. Bootstrap values from 1000 random replicates are indicated at the nodes. The length of the branches inversely correlates with the degree of similarity. Only the sequences from the extracellular domains without signal peptides and transmembrane domains were used.

Mentions: The conserved part of the sea squirt sequence with the three Ig-like domains was used to build a phylogenetic tree by the neighbour joining method (Fig. 2). In the resulting unrooted tree, the Ciona sequence is placed on one branch together with the lancelet sequence as would be expected for two members of the chordata. However, the relative distance between the sea squirt and lancelet is extremely large such that the sea squirt behaves like an outgroup.


Comparison of the receptor FGFRL1 from sea urchins and humans illustrates evolution of a zinc binding motif in the intracellular domain.

Zhuang L, Karotki AV, Bruecker P, Trueb B - BMC Biochem. (2009)

Phylogenetic analysis of the FGFRL1 sequences. An unrooted tree was built by the neighbour joining method. Bootstrap values from 1000 random replicates are indicated at the nodes. The length of the branches inversely correlates with the degree of similarity. Only the sequences from the extracellular domains without signal peptides and transmembrane domains were used.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2806250&req=5

Figure 2: Phylogenetic analysis of the FGFRL1 sequences. An unrooted tree was built by the neighbour joining method. Bootstrap values from 1000 random replicates are indicated at the nodes. The length of the branches inversely correlates with the degree of similarity. Only the sequences from the extracellular domains without signal peptides and transmembrane domains were used.
Mentions: The conserved part of the sea squirt sequence with the three Ig-like domains was used to build a phylogenetic tree by the neighbour joining method (Fig. 2). In the resulting unrooted tree, the Ciona sequence is placed on one branch together with the lancelet sequence as would be expected for two members of the chordata. However, the relative distance between the sea squirt and lancelet is extremely large such that the sea squirt behaves like an outgroup.

Bottom Line: FGFRL1, the gene for the fifth member of the fibroblast growth factor receptor (FGFR) family, is found in all vertebrates from fish to man and in the cephalochordate amphioxus.Since it does not occur in more distantly related invertebrates such as insects and nematodes, we have speculated that FGFRL1 might have evolved just before branching of the vertebrate lineage from the other invertebrates (Beyeler and Trueb, 2006).A comparison of the intracellular domain between sea urchin and human FGFRL1 provides interesting insights into the shaping of a novel zinc binding domain.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Clinical Research, University of Bern, 3010 Bern, Switzerland. lei.zhuang@dkf.unibe.ch

ABSTRACT

Background: FGFRL1, the gene for the fifth member of the fibroblast growth factor receptor (FGFR) family, is found in all vertebrates from fish to man and in the cephalochordate amphioxus. Since it does not occur in more distantly related invertebrates such as insects and nematodes, we have speculated that FGFRL1 might have evolved just before branching of the vertebrate lineage from the other invertebrates (Beyeler and Trueb, 2006).

Results: We identified the gene for FGFRL1 also in the sea urchin Strongylocentrotus purpuratus and cloned its mRNA. The deduced amino acid sequence shares 62% sequence similarity with the human protein and shows conservation of all disulfides and N-linked carbohydrate attachment sites. Similar to the human protein, the S. purpuratus protein contains a histidine-rich motif at the C-terminus, but this motif is much shorter than the human counterpart. To analyze the function of the novel motif, recombinant fusion proteins were prepared in a bacterial expression system. The human fusion protein bound to nickel and zinc affinity columns, whereas the sea urchin protein barely interacted with such columns. Direct determination of metal ions by atomic absorption revealed 2.6 mole zinc/mole protein for human FGFRL1 and 1.7 mole zinc/mole protein for sea urchin FGFRL1.

Conclusion: The FGFRL1 gene has evolved much earlier than previously assumed. A comparison of the intracellular domain between sea urchin and human FGFRL1 provides interesting insights into the shaping of a novel zinc binding domain.

Show MeSH
Related in: MedlinePlus