第1090回生物科学セミナー
A Comparative Proteomic Approach to Studying Echinoderm Skeleton Formation
Dr. Brian Livingston（California State University Long Beach）
2016年03月04日(金) 16:00-17:00 理学部2号館 201号室
The formation of hard skeletal elements evolved rapidly in many animal taxa.
Studies on the proteins involved have suggested the trait evolved independently
in many of these groups. However, the prominent skeletal proteins in disparate
animal phyla often share physical properties, including charge and repetitive
sequence elements, and are often found in families resulting from gene
duplication. The origin, role and necessity of such proteins in skeletal formation
remains unclear. More recent proteomic approaches have detected large numbers
of additional proteins present in mineralized tissues. The sheer number of
proteins found makes it difficult to ascertain their importance to skeleton
formation. The skeletal proteomes identified in sea urchins fit these patterns.
There are a large number of spicule matrix proteins that share signal sequences,
C-type lectin domains and repetitive regions of acidic amino acids. There are also
close to 400 proteins that have been identified in the various proteomes. We have
taken a comparative approach to examine the conservation of proteins in the
echinoderm skeleton. We have determined the partial skeletal proteome of two
brittle stars and the complete skeletal proteome of the sea star Patiria miniata.
Comparisons reveal that the spicule matrix proteins are unique to sea urchins,
although C-type lectin-containing proteins are found in brittle stars. Sea stars
lack these proteins. We have also identified other skeletal proteins that are
conserved between all echinoderms, as well as others unique to a specific group.
Some of the conserved proteins are also found in vertebrate bone proteomes,
suggesting a deeper connection among deuterostomes.
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