Recombinant Drosophila grimshawi Adenosine monophosphate-protein transferase FICD homolog (GH10751) is a protein that belongs to the FICD homolog family and is found in the fruit fly Drosophila grimshawi . It is involved in the transfer of adenosine monophosphate to other proteins . The recombinant form of this protein is produced using genetic engineering techniques, where the gene encoding GH10751 is inserted into a host organism (e.g., E. coli) to produce large quantities of the protein .
Adenosine Monophosphate-Protein Transferase Activity Adenosine monophosphate-protein transferase FICD homolog (GH10751) functions as a protein adenylyltransferase, catalyzing the transfer of an AMP moiety to target proteins . This post-translational modification can alter the activity, localization, or interaction of the target protein .
Relevance to Drosophila Biology In Drosophila, FICD homologs are involved in various biological processes, including neuronal development and function, signaling pathways, and responses to environmental stimuli .
Potential Research Applications Recombinant GH10751 can be used in biochemical assays to study its enzymatic activity, identify target proteins, and investigate the regulatory mechanisms in which it participates . It can also be employed in structural studies to understand the molecular basis of its function.
Recombinant GH10751 is typically produced in E. coli and purified using affinity chromatography, such as His-tag purification . Quality control measures include SDS-PAGE to assess purity and ensure that the protein is at least 85-90% pure . Proper storage and handling are crucial to maintain the protein's integrity and activity .
Biochemical Assays: Studying enzymatic activity and identifying target proteins.
Structural Studies: Understanding the molecular basis of its function.
Drug Discovery: Screening for inhibitors or activators of GH10751.
Understanding Diapause: Investigating genes associated with successful diapause in Drosophila .
Pesticide Transporter Studies: Comprehensive characterization of pesticide transporters in Drosophila melanogaster .
This protein functions as a dual-acting enzyme, mediating both the addition (AMPylation) and removal (de-AMPylation) of adenosine 5'-monophosphate (AMP) to/from target proteins. The Glu-236 residue dictates its activity as either an adenylyltransferase (AMPylation) or a phosphodiesterase (de-AMPylation). It plays a crucial regulatory role in the unfolded protein response (UPR) by modulating the AMPylation/de-AMPylation state of Hsc70-3/BiP. Under normal cellular conditions, it AMPylates Hsc70-3/BiP at Thr-518, thus inactivating it. Conversely, under endoplasmic reticulum stress, it removes the AMP moiety (de-AMPylation) from Hsc70-3/BiP at Thr-518, restoring HSPA5/BiP activity.
KEGG: dgr:Dgri_GH10751