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J. Cell Biol.,
Volume 141, Number 4, May 18, 1998 1009-1017
Peptide-binding Protein
Instituto Cajal, Consejo Superior de Investigaciones Científicas, 28002 Madrid, Spain
The characterization of scully, an essential
gene of Drosophila with phenocritical phases at embryonic and pupal stages, shows its extensive homology
with vertebrate type II L-3-hydroxyacyl-CoA dehydrogenase/ERAB. Genomic rescue demonstrates that four
different lethal mutations are scu alleles, the molecular
nature of which has been established. One of them,
scu3127, generates a nonfunctional truncated product.
scu4058 also produces a truncated protein, but it contains
most of the known functional domains of the enzyme.
The other two mutations, scu174 and scuS152, correspond
to single amino acid changes. The expression of scully mRNA is general to many tissues including the CNS;
however, it is highest in both embryonic gonadal primordia and mature ovaries and testes. Consistent with
this pattern, the phenotypic analysis suggests a role for
scully in germ line formation: mutant testis are reduced
in size and devoid of maturing sperm, and mutant ovarioles are not able to produce viable eggs. Ultrastructural analysis of mutant spermatocytes reveals the presence of cytoplasmic lipid inclusions and scarce
mitochondria. In addition, mutant photoreceptors contain morphologically aberrant mitochondria and large
multilayered accumulations of membranous material.
Some of these phenotypes are very similar to those
present in human pathologies caused by 
-oxidation
disorders.
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