F. Hamel et al., STRUCTURAL AND EVOLUTIONARY RELATIONSHIPS AMONG CHITINASES OF FLOWERING PLANTS, Journal of molecular evolution, 44(6), 1997, pp. 614-624
The analysis of nuclear-encoded chitinase sequences from various angio
sperms has allowed the categorization of the chitinases into discrete
classes. Nucleotide sequences of their catalytic domains were compared
in this study to investigate the evolutionary relationships between c
hitinase classes. The functionally distinct class III chitinases appea
r to be more closely related to fungal enzymes involved in morphogenes
is than to other plant chitinases. The ordering of other plant chitina
ses into additional classes mainly relied on the presence of auxiliary
domains--namely, a chitin-binding domain and a carboxy-terminal exten
sion--flanking the main catalytic domain. The results of our phylogene
tic analyses showed that classes I and IV form discrete and well-suppo
rted monophyletic groups derived from a common ancestral sequence that
predates the divergence of dicots and monocots. In contrast, other se
quences included in classes I and II, lacking one or both types of au
xiliary domains, were nested within class I sequences, indicating that
they have a polyphyletic origin. According to phylogenetic analyses a
nd the calculation of evolutionary rates, these chitinases probably ar
ose from different class I lineages by relatively recent deletion even
ts. The occurrence of such evolutionary trends in cultivated plants an
d their potential involvement in host-pathogen interactions are discus
sed.