Premium
A LONG‐TERM STUDY ON SEASONAL CHANGES OF GAMETIC DISEQUILIBRIUM BETWEEN ALLOZYMES AND INVERSIONS IN DROSOPHILA SUBOBSCURA
Author(s) -
Zapata Carlos,
Alvarez Gonzalo,
RodríguezTrelles Francisco,
Maside Xulio
Publication year - 2000
Publication title -
evolution
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.84
H-Index - 199
eISSN - 1558-5646
pISSN - 0014-3820
DOI - 10.1111/j.0014-3820.2000.tb00711.x
Subject(s) - biology , drosophila subobscura , disequilibrium , chromosomal inversion , population , seasonality , natural population growth , natural selection , evolutionary biology , population genetics , linkage disequilibrium , zoology , genetics , chromosome , allele , ecology , gene , karyotype , demography , haplotype , medicine , sociology , ophthalmology
Seasonal variation (spring, early summer, late summer, and autumn) of gametic disequilibrium between gene arrangements (O ST and O 3+4 ) of the O chromosome and Lap, Pept‐1 , and Acph allozyme loci, located inside these inversions, has been recorded in a natural population of Drosophila subobscura during seven years over a 15‐year period. The length of the study allowed us to investigate the temporal variation of the allozyme‐inversion associations by statistical methods of time series analysis. Cyclic seasonal changes of allozyme‐inversion associations for both Lap and Pept‐1 are detected in the natural population. In both cases, the patterns of seasonal change are due to the seasonal change of frequency of Lap and Pept‐1 allozymes occurring exclusively within the O ST gene arrangement. In contrast, the allozyme frequencies at these loci within the O 3+4 gene arrangement are stable along seasons. The patterns of temporal variation of allozyme‐inversion associations for Lap and Pept‐1 in the natural population are contrasted with those previously published that correspond to gene arrangements of the O chromosome and nucleotide polymorphism at the rp49 region located inside these inversions, suggesting that natural selection is operating on these allozyme‐inversion associations.