Going Back to Go Forward
23/03/12 14:21 Filed in: GenomeWeb Daily Scan
Submitted by S. Pelech - Kinexus on Fri, 03/23/2012 - 14:21.
One of the most tantalizing dividends of sequencing the genomes from many very diverse species is the opportunity to define the functional protein domains that are the most highly conserved in evolution. Careful alignment of the amino acids in these domains might reveal what the likely primary structures of these protein domains resembled when they first appeared in organisms on this planet. Comparison of such consensus sequences for each defined protein domain can further provide clues as to how they may have evolved from each other and ultimately how the hundreds of functional domains found within all of the known proteins may have emerged from a very small number. This molecular paleontology approach should eventually provide a protein tree of life and may even provide hints regarding the biochemistry of the earliest life forms on our planet.
At Kinexus Bioinformatics Corporation, we have recently been able to identify the predecessor of all of the typical eukaryotic protein kinases by this strategy. These findings were originally presented at the Keystone Symposium: The Evolution of Protein Phosphorylation in January 2011. We revealed that glutamine tRNA synthetase appears to be the gene from which all of the typical eukaryotic protein kinases evolved. Protein kinases form the main building components of the molecular intelligence systems of all eukaryotic cells. Interestingly, the glutamine tRNA synthase gene was also implicated as the ancestor of the choline kinases. Choline kinases catalyze the first step in the biosynthesis of phosphatidylcholine, which is the predominant phospholipid found in eukaryotic membranes. Typical protein kinases and choline kinases are not found in prokaryotes, and it may be that glutamine tRNA synthetase played a key role in the successful development of eukaryotic life from colonies of bacteria.
Link to the original blog post.
One of the most tantalizing dividends of sequencing the genomes from many very diverse species is the opportunity to define the functional protein domains that are the most highly conserved in evolution. Careful alignment of the amino acids in these domains might reveal what the likely primary structures of these protein domains resembled when they first appeared in organisms on this planet. Comparison of such consensus sequences for each defined protein domain can further provide clues as to how they may have evolved from each other and ultimately how the hundreds of functional domains found within all of the known proteins may have emerged from a very small number. This molecular paleontology approach should eventually provide a protein tree of life and may even provide hints regarding the biochemistry of the earliest life forms on our planet.
At Kinexus Bioinformatics Corporation, we have recently been able to identify the predecessor of all of the typical eukaryotic protein kinases by this strategy. These findings were originally presented at the Keystone Symposium: The Evolution of Protein Phosphorylation in January 2011. We revealed that glutamine tRNA synthetase appears to be the gene from which all of the typical eukaryotic protein kinases evolved. Protein kinases form the main building components of the molecular intelligence systems of all eukaryotic cells. Interestingly, the glutamine tRNA synthase gene was also implicated as the ancestor of the choline kinases. Choline kinases catalyze the first step in the biosynthesis of phosphatidylcholine, which is the predominant phospholipid found in eukaryotic membranes. Typical protein kinases and choline kinases are not found in prokaryotes, and it may be that glutamine tRNA synthetase played a key role in the successful development of eukaryotic life from colonies of bacteria.
Link to the original blog post.