Abstract

CREB-binding protein (p300/CBP) is a universal transcriptional co-regulator with lysine acetyltransferase activity. Drosophila melanogaster p300/CBP is a well-known regulator of embryogenesis, and recent studies in beetles and cockroaches have revealed the importance of this protein during post-embryonic development and endocrine signaling. In pest insects, p300/CBP may therefore offer a useful target for control methods based on RNA interference (RNAi). We investigated the role of p300/CBP in the pea aphid (Acyrthosiphon pisum), a notorious pest insect used as a laboratory model for the analysis of complex life-history traits. The RNAi-based attenuation of A. pisum p300/CBP significantly reduced the aphid lifespan and number of offspring, as well as shortening the reproductive phase, suggesting the manipulation of this gene contributes to accelerated senescence. Furthermore, injection of p300/CBP dsRNA also reduced the number of viable offspring and increased the number of premature nymphs, which developed in abnormally structured ovaries. Our data confirm the evolutionarily conserved function of p300/CBP during insect embryogenesis and show that the protein has a critical effect on longevity, reproduction and development in A. pisum. The potent effect of p300/CBP silencing indicates that this regulatory protein is an ideal target for RNAi-based aphid control.

Highlights

  • Protein acetylation in eukaryotes is a major post-translational modification, in which acetyl coenzyme A acts as an acetyl group donor [1,2]

  • The p300/CBP mRNA sequence from A. pisum clone LL01 was compared to the corresponding template sequence in the NCBI database (XM_003242184)

  • We found that the survival rate among the offspring of mothers injected with p300/CBP double-stranded RNA (dsRNA) was significantly lower than peers from the control group, whose mothers were injected with GFP dsRNA (Figure 6D)

Read more

Summary

Introduction

Protein acetylation in eukaryotes is a major post-translational modification, in which acetyl coenzyme A acts as an acetyl group donor [1,2]. The acetylation of proteins regulates many processes, including gene expression, cell cycle progression, development and aging [3,4]. Acetylation affects the function of proteins by conferring a positive charge, which influences stability, enzymatic activity, subcellular localization and cross-talk with other protein modifications such as methylation [4]. The acetylation of proteins is regulated by the opposing activity of lysine acetyltransferases (KATs) and lysine deacetylases (KDACs) [3,5]. A fine balance between KAT and KDAC activities maintains normal biologic functions [6], so any disruption of this balance (caused naturally or triggered by the use of inhibitors) can severely affect physiology and development [7,8,9]

Methods
Results
Conclusion
Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call