Functional characterization of the tomato Cyclin-Dependent Kinase inhibitor SlKRP1 domains involved in protein-protein interactions.
Authors: Nafati, M., Cheniclet, C., Hernould, M., Do, P.T., Fernie, A., Chevalier, C., Gévaudant, F.
Relevance of the research
Cell division, as a crucial process required for fruit growth, is negatively regulated by a class of specific inhibitors, called the Kip-Related Proteins or KRPs, for which EU-SOL scientists have made a thorough functional and structural analysis.
Focus
After successful flower pollination and fertilization, fruit growth in tomato first occurs according to a very active period of cell divisions. The molecular mechanisms regulating the cell cycle which leads to cell division or mitosis, requires the sequential involvement of protein complexes whose activity is finely tuned by specific inhibitors. These inhibitors called KRPs were identified in plants based on a very short sequence homology to the animal counterparts known to play important roles in the induction of many types of cancer when deregulated. Apart their obvious inhibitory function on cell division, still little is known about the plant KRPs at the functional and structural levels.
Results
In this manuscript EU-SOL scientists performed a functional analysis of various domains present in KRPs from tomato, using a series of deleted or recombinant proteins combined with imaging techniques to address the sub-cellular and sub-nuclear localizations of these proteins and their ability to physically interact with candidate partners involved in the cell cycle regulation. EU-SOL scientists were able to identify new functionally relevant domains in tomato KRPs relative to subcellular localization or proteolytic degradation, suggesting that these cell division inhibitors from tomato fruit may act in a similar way than the animal counterparts.
Full publication
Nafati, M., Frangne, N., Hernould, M., Chevalier, C., Gévaudant, F. (2010) Functional characterization of the tomato Cyclin-Dependent Kinase inhibitor SlKRP1 domains involved in protein-protein interactions. New Phytologist , 188: 136-149
