Methylation-dependent SUMOylation of the architectural transcription factor HMGA2
| Autor: | Åsmund K. Røhr, Thomas Sæther, Ola Myklebost, Marianne Stabell, Odd S. Gabrielsen |
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| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Polyhomeotic Lysine Amino Acid Motifs Biophysics SUMO protein Biochemistry Methylation Cell Line 03 medical and health sciences 0302 clinical medicine Protein Domains Humans Amino Acid Sequence Molecular Biology Transcription factor Binding Sites Sequence Homology Amino Acid Chemistry HMGA2 Protein Sumoylation Cell Biology Chromatin Cell biology A-site 030104 developmental biology High-mobility group 030220 oncology & carcinogenesis Ubiquitin-Conjugating Enzymes Protein Binding Transcription Factors |
| Zdroj: | Biochemical and Biophysical Research Communications-BBRC |
| ISSN: | 1090-2104 0006-291X |
| Popis: | High mobility group A2 (HMGA2) is a chromatin-associated protein involved in the regulation of stem cell function, embryogenesis and cancer development. Although the protein does not contain a consensus SUMOylation site, it is shown to be SUMOylated. In this study, we demonstrate that the first lysine residue in the reported K66KAE SUMOylation motif in HMGA2 can be methylated in vitro and in vivo by the Set7/9 methyltransferase. By editing the lysine, the increased hydrophobicity of the resulting 6-N-methyl-lysine transforms the sequence into a consensus SUMO motif. This post-translational editing dramatically increases the subsequent SUMOylation of this site. Furthermore, similar putative methylation-dependent SUMO motifs are found in a number of other chromatin factors, and we confirm methylation-dependent SUMOylation of a site in one such protein, the Polyhomeotic complex 1 homolog (PHC1). Together, these results suggest that crosstalk between methylation and SUMOylation is a general mode for regulation of chromatin function. |
| Databáze: | OpenAIRE |
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