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Open Access item Protein disorder in the centrosome correlates with complexity in cell types number
|Keywords:||Centrosome, Molecular assembly|
|Publisher:||Royal Society of Chemistry (Gran Bretaña)|
|Citation:||Molecular BioSystems 8, 353-367 (2012)|
|Abstract:||Here we study the properties and the evolution of proteins that constitute the Centrosome,
the complex molecular assembly that regulates the division and diﬀerentiation of animal cells.
We found that centrosomal proteins are predicted to be signiﬁcantly enriched in disordered and
coiled-coil regions, more phosphorylated and longer than control proteins of the same organism.
Interestingly, the ratio of these properties in centrosomal and control proteins tends to increase
with the number of cell-types. We reconstructed indels evolution, ﬁnding that indels signiﬁcantly
increase disorder in both centrosomal and control proteins, at a rate that is typically larger along
branches associated with a large growth in cell-types number, and larger for centrosomal than
for control proteins. Substitutions show a similar trend for coiled-coil, but they contribute less to
the evolution of disorder. Our results suggest that the increase in cell-types number in animal
evolution is correlated with the gain of disordered and coiled-coil regions in centrosomal proteins,
establishing a connection between organism and molecular complexity. We argue that the
structural plasticity conferred to the Centrosome by disordered regions and phosphorylation
plays an important role in its mechanical properties and its regulation in space and time.|
|Publisher version (URL):||http://dx.doi.org/10.1039/c1mb05199g|
|Appears in Collections:||(CBM) Artículos|
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