Michl-Holzinger, Philipp and Obermeyer, Simon and Markusch, Hanna and Pfab, Alexander and Ettner, Andreas and Bruckmann, Astrid and Babl, Sabrina and Laengst, Gernot and Schwartz, Uwe and Tvardovskiy, Andrey and Jensen, Ole N. and Osakabe, Akihisa and Berger, Frederic and Grasser, Klaus D. (2022) Phosphorylation of the FACT histone chaperone subunit SPT16 affects chromatin at RNA polymerase II transcriptional start sites in Arabidopsis. NUCLEIC ACIDS RESEARCH, 50 (9). pp. 5014-5028. ISSN 0305-1048, 1362-4962
Full text not available from this repository. (Request a copy)Abstract
The heterodimeric histone chaperone FACT, consisting of SSRP1 and SPT16, contributes to dynamic nucleosome rearrangements during various DNA-dependent processes including transcription. In search of post-translational modifications that may regulate the activity of FACT, SSRP1 and SPT16 were isolated from Arabidopsis cells and analysed by mass spectrometry. Four acetylated lysine residues could be mapped within the basic C-terminal region of SSRP1, while three phosphorylated serine/threonine residues were identified in the acidic C-terminal region of SPT16. Mutational analysis of the SSRP1 acetylation sites revealed only mild effects. However, phosphorylation of SPT16 that is catalysed by protein kinase CK2, modulates histone interactions. A non-phosphorylatable version of SPT16 displayed reduced histone binding and proved inactive in complementing the growth and developmental phenotypes of spt16 mutant plants. In plants expressing the non-phosphorylatable SPT16 version we detected at a subset of genes enrichment of histone H3 directly upstream of RNA polymerase II transcriptional start sites (TSSs) in a region that usually is nucleosome-depleted. This suggests that some genes require phosphorylation of the SPT16 acidic region for establishing the correct nucleosome occupancy at the TSS of active genes.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PROTEIN-KINASE CK2; INTRINSICALLY DISORDERED REGION; FACTORS REPRESS TRANSCRIPTION; MOBILITY GROUP BOX; DNA-BINDING; GENE-EXPRESSION; HMG DOMAIN; NUCLEOSOMAL DNA; PLANT-GROWTH; ELONGATION; |
| Subjects: | 500 Science > 570 Life sciences 500 Science > 580 Botanical sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Pflanzenwissenschaften > Lehrstuhl für Zellbiologie und Pflanzenphysiologie (Prof. Dr. Klaus Grasser) Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie I Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie III > Prof. Dr. Gernot Längst |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 14 Feb 2024 07:27 |
| Last Modified: | 14 Feb 2024 07:27 |
| URI: | https://pred.uni-regensburg.de/id/eprint/57265 |
Actions (login required)
 |
View Item |
