Genetics, Vol 132, 519-528, Copyright © 1992

INVESTIGATIONS

Characterization of Mutant Alleles of myospheroid, the Gene Encoding the {beta} Subunit of the Drosophila PS Integrins

T. A. Bunch, S. Salatino, M. C. Engelsgjerd, L. Mukai, R. F. West and D. L. Brower
Department of Molecular and Cellular Biology and Department of Biochemistry, University of Arizona, Tucson, Arizona 85721

This paper presents the characterization of nine alleles of myospheroid, which encodes the {beta}(PS) subunit of the Drosophila PS integrins. On Southern blots, the mys(XB87), mys(XN101) and mys(XR04) genes yield restriction digest patterns similar to that seen for wild-type chromosomes, however the mys(1) and mys(XG43) genes contain detectable deletions. mys(1), mys(XB87) and mys(XG43) make little or no stable protein product, and genetically behave as strong lethal alleles. For the mys(XN101) mutation, protein product is seen on immunoblots and a reduced amount of {beta}(PS) protein is seen at muscle attachment sites of embryos; this mutant protein retains some wild-type function, as revealed by complementation tests with weak alleles. Protein is also seen on immunoblots from mys(XR04) embryos, and this allele behaves as an antimorph, being more deleterious in some crosses than the complete deficiency for the locus. mys(ts2) and mys(nj42) are typically lethal in various combinations with other alleles at high temperatures only, but even at high physiological temperatures, neither appears to eliminate gene function completely. The complementation behaviors of mys(ts1) and mys(ts3) are quite unusual and suggest that these mutations involve regulatory phenomena. For mys(ts3), the data are most easily explained by postulating transvection effects at the locus. The results for mys(ts1) are less straightforward, but point to the possibility of a chromosome pairing-dependent negative interaction.

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