Temperature-dependent kinetic variation among phosphoglucose isomerase allozymes from the wing-polymorphic water strider, Limnoporus canaliculatus.
نویسنده
چکیده
Phosphoglucose isomerase (PGI) allozymes were isolated from the wing-polymorphic water strider, Limnoporus canaliculatus, and were characterized biochemically with respect to temperature-dependent kinetic and thermostability properties. At higher temperatures, the allozymes exhibited significant differences in Michaelis constant (Km) values for substrates of both the forward and reverse reaction directions. Results were consistent with expectations of adaptive kinetic differentiation based on the latitudinal variation of PGI allele frequencies. PGI genotypes also differed with regard to maximal velocity (Vmax)/Km ratios at higher temperatures. These differences were due primarily, if not exclusively, to allozyme-dependent variation in Km values. The allozymes also exhibited dramatic differences in thermostability. However, no thermostability differences were observed when the substrate analogue 6-phosphogluconate was present in the incubation medium. The data from this study, together with data from Mytilus edulis and Metridium senile on temperature-dependent kinetic variation among PGI allozymes, form a consistent picture of natural selection influencing the clinal variation of alleles at this locus in these three phylogenetically distant organisms. More definitive support of this hypothesis, however, must await additional studies on the physiological effects of the allozymic variation as well as direct measurements of fitness differences among the enzyme genotypes.
منابع مشابه
Phosphoglucose Isomerase Variability in Sympatric Populations of Mediterranean Species
Genetic variability at the phosphoglucose isomerase (PGI) locus was compared in Mediterranean sympatric populations of Patella aspera, P. coerulea and P. lusitan~ca. P. aspera and P. coerulea show PG1 patterns much alike, while P. lusitanica exhibits a more anodal general zone of mobility of its PG1 allozymes. The differentiation of P. lusitanica pattern may be tentatively interpreted as the re...
متن کاملGenetic and Environmental Determinants of Wing Polymorphism in the Waterstrider Limnoporus Canaliculatus.
متن کامل
Structural and functional differentiation of two clinally distributed glucosephosphate isomerase allelic isozymes from the teleost Fundulus heteroclitus.
The teleost Fundulus heteroclitus (L.) possesses two loci, Gpi-A and Gpi-B, for the glycolytic enzyme, glucose-phosphate isomerase (GPI; D-glucose-6-phosphate ketol-isomerase; E.C. 5.3.1.9). The Gpi-B locus is polymorphic in Fundulus, with two common alleles, Gpi-Bb and Gpi-Bc, distributed in a clinal manner in populations along the east coast of North America. Since this clinal distribution is...
متن کاملAdaptation at Specific Loci. III. Field Behavior and Survivorship Differences among Colias Pgi Genotypes Are Predictable from IN VITRO Biochemistry.
Previous work on the phosphoglucose isomerase (PGI) polymorphism of Colias butterflies led to predictions concerning aspects of differential survivorship and fecundity among the polymorphic genotypes in the wild. Explicit assumptions underlying these predictions were that functional differences among genotypes at the in vitro biochemical level reflected roughly corresponding differences in vivo...
متن کاملAdaptation at Specific Loci. VI. Divergence vs. Parallelism of Polymorphic Allozymes in Molecular Function and Fitness-Component Effects Among CO&H Species (Lepidoptera, Pieridae)
In lowland Cobs butterflies, genotypes of the enzyme phosphoglucose isomerase (PGI) show major differences in molecular function, from which genotypic differences in organismal performance and fitness components in the wild are accurately predictable. The alpine species Colias meadii seems to share electromorph alleles with lowland congeners at PGI and phosphoglucomutase (PGM). However, high-re...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Molecular biology and evolution
دوره 4 3 شماره
صفحات -
تاریخ انتشار 1987