Type-I Prenyl Protease Function Is Required in the Male Germline of Drosophila melanogaster

G3: Genes, Genomes, Genetics

Sara Kevorkian¹  Amanda Amell¹  Katie Adolphsen¹  Kyle Mears¹  Dietmar Schwarz¹  Sandra R. Schulze¹  Nathan Havko¹  Hayley Neher¹ 

[1] Biology Department, Western Washington University, Bellingham, Washington 98225Biology Department, Western Washington University, Bellingham, Washington 98225Biology Department, Western Washington University, Bellingham, Washington 98225

关键词: prenylation;    human disease;    fertility;    molecular evolution;    mutagenesis;   

DOI  :  10.1534/g3.112.002188

学科分类：生物科学（综合）

来源: Genetics Society of America

【 摘 要 】

Many proteins require the addition of a hydrophobic prenyl anchor (prenylation) for proper trafficking and localization in the cell. Prenyl proteases play critical roles in modifying proteins for membrane anchorage. The type I prenyl protease has a defined function in yeast (Ste24p/Afc1p) where it modifies a mating pheromone, and in humans (Zmpste24) where it has been implicated in a disease of premature aging. Despite these apparently very different biological processes, the type I prenyl protease gene is highly conserved, encoded by a single gene in a wide range of animal and plant groups. A notable exception is Drosophila melanogaster, where the gene encoding the type I prenyl protease has undergone an unprecedented series of duplications in the genome, resulting in five distinct paralogs, three of which are organized in a tandem array, and demonstrate high conservation, particularly in the vicinity of the active site of the enzyme. We have undertaken targeted deletion to remove the three tandem paralogs from the genome. The result is a male fertility defect, manifesting late in spermatogenesis. Our results also show that the ancestral type I prenyl protease gene in Drosophila is under strong purifying selection, while the more recent replicates are evolving rapidly. Our rescue data support a role for the rapidly evolving tandem paralogs in the male germline. We propose that potential targets for the male-specific type I prenyl proteases include proteins involved in the very dramatic cytoskeletal remodeling events required for spermatid maturation.

【 授权许可】

Unknown