Biology
Phospholipase C-γ contains introns shared by src homology 2 domains in many unrelated proteins
Document Type
Article
Abstract
Many proteins with novel functions were created by exon shuffling around the time of the metazoan radiation. Phospholipase C-γ (PLC-γ) is typical of proteins that appeared at this time, containing several different modules that probably originated elsewhere. To gain insight into both PLC-γ evolution and structure-function relationships within the Drosophila PLC-γ encoded by small swing (sl), we cloned and sequenced the PLC-γ homologs from Drosophila pseudoobscura and D. virilis and compared their gene structure and predicted amino acid sequences with PLC-γ homologs in other animals. PLC-γ has been well conserved throughout, although structural differences suggest that the role of tyrosine phosphorylation in enzyme activation differs between vertebrates and invertebrates. Comparison of intron positions demonstrates that extensive intron loss has occurred during invertebrate evolution and also reveals the presence of conserved introns in both the N- and C-terminal PLC-γ SH2 domains that are present in SH2 domains in many other genes. These and other conserved SH2 introns suggest that the SH2 domains in PLC-γ are derived from an ancestral domain that was shuffled not only into PLC-γ, but also into many other unrelated genes during animal evolution.
Publication Title
Genetics
Publication Date
6-2003
Volume
164
Issue
2
First Page
433
Last Page
442
ISSN
0016-6731
DOI
10.1093/genetics/164.2.433
Keywords
Phospholipase C-γ, Drosophila
Repository Citation
Manning, Charlene M.; Mathews, Wendy R.; Fico, Leah P.; and Thackeray, Justin R., "Phospholipase C-γ contains introns shared by src homology 2 domains in many unrelated proteins" (2003). Biology. 398.
https://commons.clarku.edu/faculty_biology/398
Cross Post Location
Student Publications