Rapid evolution of pearl oyster shell matrix proteins with repetitive, low-complexity domains

McDougall, Carmel, Aguilera, Felipe and Degnan, Bernard M. (2013) Rapid evolution of pearl oyster shell matrix proteins with repetitive, low-complexity domains. Journal of the Royal Society Interface, 10 82: 20130041.-20130041.10. doi:10.1098/rsif.2013.0041


Author McDougall, Carmel
Aguilera, Felipe
Degnan, Bernard M.
Title Rapid evolution of pearl oyster shell matrix proteins with repetitive, low-complexity domains
Journal name Journal of the Royal Society Interface   Check publisher's open access policy
ISSN 1742-5689
1742-5662
Publication date 2013-05
Sub-type Article (original research)
DOI 10.1098/rsif.2013.0041
Volume 10
Issue 82
Start page 20130041.
End page 20130041.10
Total pages 10
Place of publication London, United Kingdom
Publisher The Royal Society Publishing
Collection year 2014
Language eng
Abstract The lysine (K)-rich mantle protein (KRMP) and shematrin protein families are unique to the organic matrices of pearl oyster shells. Similar to other proteins that are constituents of tough, extracellular structures, such as spider silk, shematrins and KRMPs, contain repetitive, low-complexity domains (RLCDs). Comprehensive analysis of available gene sequences in three species of pearl oyster using BLAST and hidden Markov models reveal that both gene families have large memberships in these species. The shematrin gene family expanded before the speciation of these oysters, leading to a minimumof eight orthology groups. By contrast, KRMPs expanded primarily after speciation leading to species-specific gene repertoires. Regardless of their evolutionary history, the rapid evolution of shematrins and KRMPs appears to be the result of the intrinsic instability of repetitive sequences encoding the RLCDs, and the gain, loss and shuffling of other motifs. This mode of molecular evolution is likely to contribute to structural characteristics and evolvability of the pearl oyster shell. Based on these observations, we infer that analogous RLCD proteins throughout the animal kingdom also have the capacity to rapidly evolve and as a result change their structural properties.
Keyword Biomineralization
Lysine (K)-rich mantle protein
Mollusc
Oyster
Pinctada
Shematrin
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Article number 20130041

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2014 Collection
School of Biological Sciences Publications
 
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