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Fused Rola Protein Enhances β-Glucoronidase Activity 50-Fold: Implication for Rola Mechanism of Action

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We report that the plant oncoprotein RolA from Agrobacterium rhizogenes acts to stabilize β- glucoronidase (Gus) when the two proteins are expressed as a fusion protein in transformed tobacco. The observed 50-fold increase of Gus activity was shown to be related to protein accumulation, with no significant changes in mRNA abundance, kinetic properties of the enzyme and thermostability. The entire RolA sequence is essential to achieve the full effect since both the N-terminal region, spanning a putative reverse signal-anchor and nuclear targeting sequences, or the contiguous C-terminal portion were shown to increase Gus activity only 10-fold. A possible interference of RolA in the protein degradation pathway regulated by auxin is discussed.

Keywords: enzyme activity; glucuronidase; protein accumulation; protein thermal stability; rola protein; translational fusion

Document Type: Review Article


Publication date: June 1, 2003

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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