The Recombinant Acanthamoeba polyphaga mimivirus Uncharacterized Protein R468, referred to as MIMI_R468, is a protein derived from the Acanthamoeba polyphaga mimivirus (APMV), a giant virus known for its complex genome and diverse protein composition. MIMI_R468 is expressed in Escherichia coli (E. coli) and is tagged with a His-tag for easy purification and identification. This protein is part of the extensive proteome of APMV, which includes over 900 proteins, many of which remain uncharacterized in terms of their specific functions .
Protein Length and Expression: MIMI_R468 is a full-length protein consisting of 240 amino acids. It is expressed in E. coli, which is a common host for recombinant protein production due to its efficiency and cost-effectiveness .
Tagging: The protein is fused with an N-terminal His-tag, facilitating its purification using affinity chromatography techniques .
Species Origin: The protein originates from Acanthamoeba polyphaga mimivirus, a virus known for infecting amoebas and possessing a large genome that encodes numerous proteins .
MIMI_R468 is involved in several biochemical pathways, although its specific roles within these pathways are not fully understood. It interacts with other proteins and molecules, which can be identified through techniques like yeast two-hybrid assays, co-immunoprecipitation, and pull-down assays . Understanding these interactions is crucial for elucidating the protein's functions and its potential applications in research.
To effectively communicate research findings related to MIMI_R468, data should be presented in a clear and concise manner, often using tables and figures to highlight key results. Tables are particularly useful for displaying numerical data, while figures can illustrate trends and relationships between variables .
| Characteristic | Description |
|---|---|
| Protein Length | 240 amino acids |
| Expression Host | E. coli |
| Tag | N-terminal His-tag |
| Species Origin | Acanthamoeba polyphaga mimivirus |
A figure could illustrate the process of expressing MIMI_R468 in E. coli and its subsequent purification using affinity chromatography. This would visually represent the steps involved in obtaining the recombinant protein.
Future studies on MIMI_R468 could focus on elucidating its specific biochemical functions and its interactions with other proteins within the APMV proteome. Techniques such as RNA interference or protein silencing could be employed to assess the protein's role in viral replication and host-virus interactions . Additionally, structural analysis through X-ray crystallography could provide insights into the protein's structure and potential binding sites, further informing its functional characterization.