Nuclear and nucleolar targeting sequences of c-erb-A, c-myb, N-myc, p53, HSP70, and HIV tat proteins
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Discussion
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Implication
Experimental study identifies specific nuclear and nucleolar targeting peptide sequences across multiple oncoproteins and viral regulators, highlighting structural motifs necessary for subcellular...
Key Points
- To identify and functionally evaluate peptide motifs within specific viral proteins, heat-shock proteins, and oncoproteins that direct transport to the cell nucleus or nucleolus.
- Predicted potential nuclear localization sequences within c-myb, N-myc, p53, c-erb-A, HIV Tat, and HSP70 based on consensus peptide motifs.
- Constructed fusion genes linking candidate targeting sequences to the cytoplasmic reporter enzyme pyruvate kinase and transfected them into cultured cells to monitor localization.
- Identified distinct peptides within c-myb (PLLKKIKQ), N-myc (PPQKKIKS), p53 (PQPKKKP), and c-erb-A (SKRVAKRKL) that efficiently target pyruvate kinase into the cell nucleus.
- Demonstrated that a 12-amino-acid peptide from HIV Tat (GRKKRRQRRRAP) and an 18-amino-acid sequence from HSP70 direct reporter protein accumulation in the nucleolus.
- Showed that combining the c-Myc nuclear localization signal with the basic COOH-terminal region of Tat targets fusion proteins to both the nucleus and nucleolus.
Cite This Study
Dang et al. (1989) studied this question.