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Expression artifact with retroviral vectors based on pBMN.
Yoshitaka Fukunaga1, Robert A Svoboda, Ronald L Cerny
1Department of Oral Biology, University of Nebraska Medical Center, Omaha, 68198, USA.
Analytical Biochemistry
|July 16, 2009
Summary
Researchers discovered a novel artifact in p120 catenin studies. A higher molecular weight form was identified as a fusion protein due to discrepancies in retroviral vector sequences, not a posttranslational modification.
Area of Science:
- Molecular Biology
- Cell Biology
- Protein Biochemistry
Background:
- p120 catenin is a key regulator of cell-cell adhesion.
- Alternative splicing generates diverse p120 catenin isoforms.
- Posttranslational modifications can alter protein function and molecular weight.
Purpose of the Study:
- To investigate a novel, higher molecular weight form of p120 catenin observed during splice form characterization.
- To determine if this form represents a new posttranslational modification or an experimental artifact.
Main Methods:
- Analysis of p120 catenin splice variants.
- Protein gel electrophoresis to assess molecular weight.
- Sequence analysis of retroviral vectors and expressed proteins.
Main Results:
- A higher molecular weight form of p120 catenin was detected, dependent on splicing.
- This form was identified as a fusion protein resulting from the retroviral vector sequence.
- Discrepancies were found between the experimental vector sequence and its publicly available counterpart.
Conclusions:
- The observed higher molecular weight form of p120 catenin is an artifact, not a novel posttranslational modification.
- Investigational caution is advised regarding potential sequence discrepancies in retroviral vectors.
- Accurate vector sequencing is critical for interpreting experimental results in molecular biology studies.
