Molecular basis of intracistronic complementation in the Passover locus of Drosophila.
The only demonstrated mechanism for intracistronic genetic complementation requires physical interaction of protein subunits to create a functional molecule. We demonstrate another and perhaps quite general mechanism utilizing proteins with unique and shared domains. The Drosophila neural mutant Passover (Pas) disrupts specific synaptic connections. Alleles of a lethal complementation group exhibit a complex pattern of complementation with Pas alleles. Whereas all heterozygotes between these lethal alleles and Pas are viable, only some alleles complement the neural defect of Pas. Lethal and neural functions are separately encoded by two proteins that have distinct N-terminal domains and a common C-terminal portion. Neural-specific and lethal-specific mutations map to unique exons, while neural-lethal mutations map to shared exons. Combinations of lethal and neural alleles result in production of both proteins and demonstrate intracistronic complementation.
Krishnan
S N
SN
Department of Biology, Yale University, New Haven, CT 06511.
Frei
E
E
Schalet
A P
AP
Wyman
R J
RJ
D000483:Alleles; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002874:Chromosome Mapping; D003001:Cloning, Molecular; D017630:Connexins / Q000235:genetics*; D004330:Drosophila / Q000235:genetics* / Q000502:physiology; D029721:Drosophila Proteins; D004558:Electric Stimulation; D005091:Exons; D005816:Genetic Complementation Test; D006579:Heterozygote; D007438:Introns; D046911:Macromolecular Substances; D008957:Models, Genetic; D008969:Molecular Sequence Data; D009046:Motor Neurons / Q000502:physiology*; D009132:Muscles / Q000294:innervation*; D009419:Nerve Tissue Proteins / Q000235:genetics*; D016133:Polymerase Chain Reaction; D015183:Restriction Mapping; D017386:Sequence Homology, Amino Acid
D017630:Connexins; D029721:Drosophila Proteins; D046911:Macromolecular Substances; D009419:Nerve Tissue Proteins; C079324:shakB protein, Drosophila