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[Analysis of the mutations induced by alkylating compounds in Drosophila sperm. II. The nature of the chemically induced unstable locus states in Drosophila melanogaster].

Two types of unstable visible mutations induced by ethylnitrosourea and ethylmethanesulfonate were detected and studied. In cases of replicating instability, mutations newly emerging in the offspring of a single male were allelic. They were located either in a single site or in different sites of the gene. Substitution of autosomes in unstable lines was followed by stabilization of both normal and mutant phenotype in two cases of replicating instability.

Alkylating Agents↗

[Time of gene activity in ontogenesis of Drosophila. 2. Temperature-sensitive period of SSa-40a mutation in Drosophila melanogaster].

In the mutants aristapedia (ssa-40a) of D. melanogaster, the temperature-sensitive period (TSP) was determined for the effects observed in the thoracic legs (fusion of tarsal segments). The TSP began in the middle of the first and finished in the end of the second quarter of the 3rd larval instar. The TSP for ssa-40a overlapped the TSP for homoeotic transformation of aristae into tarsi but did not overlap the TSP for spineless effects. An attempt is undertaken to consider the state of determinantion on the basis of the hypothesis of autogenous regulation of gene activity.

Alleles↗

[An electron microscopic study of the structure of the spermatozoa from sterile males from a crossing of Drosophila virilis x Drosophila lummei].

Using electron microscope, we have studied structure of the tail region of developing spermatozoa in sterile hybrid males FB1 and F2 resulting from D. virilis x D. lummei crosses, as well as in fertile males of D. virilis. Multiple disturbances in the structure of spermatid plasma membrane have been found in sterile males. The membrane is interrupted in many points; this is particularly apparent in the outer thicker layer. The adjacent nucleus (AN) of spermatids of hybrids also differs from that in D. virilis spermatid. The crystalline ultrastructure in this case has a lower volume as compared with D. virilis, it is located asymmetrically within the AN and is displaced to the edge of that part of the AN, which is located closely to the bundle of contractile fibrils. At the stage of elongation, nonuniform inclusions of irregular shape, several times larger than globules of the crystalline structure, are located nonuniformly within this crystal-like structure. The membrane of the AN is interrupted in many points or is fully absent. Matrix consisting of a large number of small globules is distributed nonuniformly within the AN. It is concluded that the presence of multiple disturbances of spermatid ultra-structure is the main factor leading to lack of sperm mobility and, correspondingly, sterility of virilis-lummei hybrid males.

Animals↗

Differences and similarities between Drosophila and mammalian 3' end processing of histone pre-mRNAs.

We used nuclear extracts from Drosophila Kc cells to characterize 3' end processing of Drosophila histone pre-mRNAs. Drosophila SLBP plays a critical role in recruiting the U 7 snRNP to the pre-mRNA and is essential for processing all five Drosophila histone pre-mRNAs. The Drosophila processing machinery strongly prefers cleavage after a fourth nucleotide following the stem-loop and favors an adenosine over pyrimidines in this position. Increasing the distance between the stem-loop and the HDE does not result in a corresponding shift of the cleavage site, suggesting that in Drosophila processing the U 7 snRNP does not function as a molecular ruler. Instead, SLBP directs the cleavage site close to the stem-loop. The upstream cleavage product generated in Drosophila nuclear extracts contains a 3' OH, and the downstream cleavage product is degraded by a nuclease dependent on the U 7 snRNP, suggesting that the cleavage factor has been conserved between Drosophila and mammalian processing. A 2'O-methyl oligonucleotide complementary to the first 17 nt of the Drosophila U 7 snRNA was not able to deplete the U 7 snRNP from Drosophila nuclear extracts, suggesting that the 5' end of the Drosophila U 7 snRNA is inaccessible. This oligonucleotide selectively inhibited processing of only two Drosophila pre-mRNAs and had no effect on processing of the other three pre-mRNAs. Together, these studies demonstrate that although Drosophila and mammalian histone pre-mRNA processing share common features, there are also significant differences, likely reflecting divergence in the mechanism of 3' end processing between vertebrates and invertebrates.

Animals↗