Molecular Biology and Evolution, Vol 12, 123-130, Copyright © 1995 by Society for Molecular Biology and Evolution
K Kuma, N Iwabe and T Miyata
In the protein kinase family, the basic function of kinase domain is
similar among members. According to the standard view of functional
constraint, the molecular evolutionary rate depends on functional and
structural features characteristic of individual molecules (local
constraint). Thus the evolutionary rate of the kinase domain is expected to
be similar for different members. Contrary to this expectation, a
comparison of the evolutionary rates revealed a wide difference among
members; it amounts to about 100 times difference between the maximum and
minimum rates. A similar result was also found in members of the
immunoglobulin (Ig) family. In addition, significant correlations in
evolutionary rate were observed between the kinase domain and the Ig-like
domain in the receptor protein tyrosine kinases and between the kinase
domain and the SH domain in the nonreceptor-type kinases. Furthermore, the
evolutionary rates of family members that are expressed tissue specifically
differ widely, depending on their tissue distribution: members expressed in
the brain evolve with significantly slower rates than those expressed in
the immune system. These results strongly suggest the presence of an
alternative constraint (global constraint) against changes on molecules
derived from higher levels like tissues or organs.
ORIGINAL ARTICLE
Functional constraints against variations on molecules from the tissue level: slowly evolving brain-specific genes demonstrated by protein kinase and immunoglobulin supergene families
Department of Biophysics, Faculty of Science, Kyoto University, Japan.
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