Four differently chromatin-associated maize HMG domain proteins modulate DNA structure and act as architectural elements in nucleoprotein complexes
| Autor: | Rudi Grimm, Klaus D. Grasser, Christoph Ritt, Silvia Fernández, Juan C. Alonso |
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| Rok vydání: | 1998 |
| Předmět: |
DNA
Plant Spermidine Plant Science Biology Polymerase Chain Reaction Zea mays DNA-binding protein law.invention chemistry.chemical_compound law Ethidium Genetics DNA Primers DNA Superhelical High Mobility Group Proteins HMGA Cell Biology Chromatin Recombinant Proteins Nucleoprotein DNA-Binding Proteins Kinetics Nucleoproteins Biochemistry chemistry Recombinant DNA DNA supercoil Ethidium bromide DNA |
| Zdroj: | Ritt, C, Grimm, R, Fernandéz, S, Alonso, J C & Grasser, K D 1998, ' Four Differently Chromatin-Associated Maize HMG Domain Proteins Modulate DNA Structure and Act as Architectural Elements in Nucleoprotein Complexes ', Plant Journal, vol. 14, pp. 623-631 . |
| ISSN: | 1365-313X 0960-7412 |
| DOI: | 10.1046/j.1365-313x.1998.00154.x |
| Popis: | In contrast to other eukaryotes which usually express two closely related HMG1-like proteins, plant cells have multiple relatively variable proteins of this type. A systematic analysis of the DNA-binding properties of four chromosomal HMG domain proteins from maize revealed that they bind linear DNA with similar affinity. HMGa, HMGc1/2 and HMGd specifically recognise diverse DNA structures such as DNA mini-circles and supercoiled DNA. They induce DNA-bending, and constrain negative superhelical turns in DNA. In the presence of DNA, the HMG domain proteins can self-associate, whereas they are monomeric in solution. The maize HMG1-like proteins have the ability to facilitate the formation of nucleoprotein structures to different extents, since they can efficiently replace a bacterial chromatin-associated protein required for the site-specific beta-mediated recombination. A variable function of the HMG1-like proteins is indicated by their differential association with maize chromatin, as judged by their 'extractability' from chromatin with spermine and ethidium bromide. Collectively, these findings suggest that the various plant chromosomal HMG domain proteins could be adapted to act in different nucleoprotein structures in vivo. |
| Databáze: | OpenAIRE |
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