Stott, Katherine and Watson, Matthew and Bostock, Mark J. and Mortensen, Simon A. and Travers, Andrew and Grasser, Klaus D. and Thomas, Jean O. (2014) Structural Insights into the Mechanism of Negative Regulation of Single-box High Mobility Group Proteins by the Acidic Tail Domain. JOURNAL OF BIOLOGICAL CHEMISTRY, 289 (43). pp. 29817-29826. ISSN 0021-9258, 1083-351X
Full text not available from this repository. (Request a copy)Abstract
Background: HMG-box proteins bind and bend DNA, regulated by their acidic C-terminal tails. Results: The acidic tails of HMG-D (Drosophila) and ZmHMGB1 (maize) occlude the DNA-binding regions; the strength of the interaction is phosphorylation-dependent. Conclusion: Phosphorylation provides an additional mode of negative regulation. Significance: Phosphorylation of the tails of insect and plant HMG-box proteins may modulate chromatin structure and accessibility. The Drosophila and plant (maize) functional counterparts of the abundant vertebrate chromosomal protein HMGB1 (HMG-D and ZmHMGB1, respectively) differ from HMGB1 in having a single HMG box, as well as basic and acidic flanking regions that vary greatly in length and charge. We show that despite these variations, HMG-D and ZmHMGB1 exist in dynamic assemblies in which the basic HMG boxes and linkers associate with their intrinsically disordered, predominantly acidic, tails in a manner analogous to that observed previously for HMGB1. The DNA-binding surfaces of the boxes and linkers are occluded in auto-inhibited forms of the protein, which are in equilibrium with transient, more open structures that are binding-competent. This strongly suggests that the mechanism of auto-inhibition may be a general one. HMG-D and ZmHMGB1 differ from HMGB1 in having phosphorylation sites in their tail and linker regions. In both cases, in vitro phosphorylation of serine residues within the acidic tail stabilizes the assembled form, suggesting another level of regulation for interaction with DNA, chromatin, and other proteins that is not possible for the uniformly acidic (hence unphosphorylatable) tail of HMGB1.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | DNA-BINDING PROPERTIES; GROUP CHROMOSOMAL-PROTEINS; TRANSCRIPTION FACTOR DOF2; TANDEM HMG BOXES; HISTONE H1; NMR-SPECTROSCOPY; DROSOPHILA-MELANOGASTER; REGIONS FLANKING; KINASE CK2; CHROMATIN; Chromatin; Intrinsically Disordered Protein; Nuclear Magnetic Resonance (NMR); Phosphorylation; Protein Kinase C (PKC); HMGB Protein; Acidic Regulatory Domain; Casein Kinase 2 (CK2); Paramagnetic Relaxation Enhancement; Protein Kinase C |
| Subjects: | 500 Science > 580 Botanical sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Pflanzenwissenschaften |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 12 Aug 2019 07:22 |
| Last Modified: | 12 Aug 2019 07:22 |
| URI: | https://pred.uni-regensburg.de/id/eprint/9334 |
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