Immortal coils: conserved dimerization motifs of the Drosophila ovulation prohormone ovulin.
Dimerization is an important feature of the function of some proteins, including prohormones. For proteins whose amino acid sequences evolve rapidly, it is unclear how such structural characteristics are retained biochemically. Here we address this question by focusing on ovulin, a prohormone that induces ovulation in Drosophila melanogaster females after mating. Ovulin is known to dimerize, and is one of the most rapidly evolving proteins encoded by the Drosophila genome. We show that residues within a previously hypothesized conserved dimerization domain (a coiled-coil) and a newly identified conserved dimerization domain (YxxxY) within ovulin are necessary for the formation of ovulin dimers. Moreover, dimerization is conserved in ovulin proteins from non-melanogaster species of Drosophila despite up to 80% sequence divergence. We show that heterospecific ovulin dimers can be formed in interspecies hybrid animals and in two-hybrid assays between ovulin proteins that are 15% diverged, indicating conservation of tertiary structure amidst a background of rapid sequence evolution. Our results suggest that because ovulin's self-interaction requires only small conserved domains, the rest of the molecule can be relatively tolerant to mutations. Consistent with this view, in comparisons of 8510 proteins across 6 species of Drosophila we find that rates of amino acid divergence are higher for proteins with coiled-coil protein-interaction domains than for non-coiled-coil proteins.
Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.
Alex
A
Wong
Adam B
AB
Christopher
Norene A
NA
Buehner
Mariana F
MF
Wolfner
D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence; D004330:Drosophila / Q000235:genetics*; D029721:Drosophila Proteins / Q000235:genetics*; D019143:Evolution, Molecular; D005260:Female; D036341:Intercellular Signaling Peptides and Proteins; D008297:Male; D008969:Molecular Sequence Data; D010455:Peptides / Q000235:genetics*; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization; D013045:Species Specificity
C489171:Acp26Aa protein, Drosophila; D029721:Drosophila Proteins; D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides