Molecular Biology and Evolution, Vol 11, 106-119, Copyright © 1994 by Society for Molecular Biology and Evolution
CN White, LE Hightower and RJ Schultz
Analysis of the heat-shock proteins (hsps) of six closely related species
of Poeciliopsis demonstrated the existence of biochemical diversity in the
hsp100, hsp70, hsp60, and hsp30 protein families among species. Each
species expressed five to seven hsp70-related isoforms. Constitutive 70-kD
isoforms were identical among species, but four different patterns of
heat-inducible isoforms were seen in these six species. Members of the
hsp70 family of molecular chaperones are included among the most highly
conserved proteins known, and the possibility of variation in hsp70 among
closely related species has rarely been addressed. The hsp30 family is
known to be less conserved than the hsp70 family, and, as expected, the
Poeciliopsis hsp30 patterns showed more variation. Most of the hsp30
isoforms characteristic of a particular species were unique to that
species. Hsp100 and hsp60 were identical in five of the species, but
alternate isoforms were found in P. monacha. The small size and limited
geographical distribution of the P. monacha population have probably
contributed to the uniqueness of the monacha pattern. Two of the species
were shown to acquire thermotolerance, the ability to withstand normally
lethal temperatures when subjected to a gradual temperature increase.
Rapid-heating protocols commonly used to establish critical thermal maxima
of organisms do not include this inducible component of thermoresistance
and therefore do not adequately assess an organism's capacity to withstand
thermal stress.
ORIGINAL ARTICLE
Variation in heat-shock proteins among species of desert fishes (Poeciliidae, Poeciliopsis)
Marine/Freshwater Biomedical Sciences Center, University of Connecticut, Storrs 06269-3044.
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