2ZFU

Structure of the methyltransferase-like domain of nucleomethylin

Summary for 2ZFU

• Entry DOI: 10.2210/pdb2zfu/pdb
• Descriptor: Cerebral protein 1, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• Functional Keywords: nucleolar protein, sam-binding protein, protein structure, nucleus, phosphoprotein, nuclear protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus, nucleolus: O43159
• Total number of polymer chains: 2
• Total formula weight: 49362.83

Authors

Minami, H.,Hashimoto, H.,Murayama, A.,Yanagisawa, J.,Sato, M.,Shimizu, T. (deposition date: 2008-01-14, release date: 2008-12-02, Last modification date: 2024-03-13)

Primary citation

Murayama, A.,Ohmori, K.,Fujimura, A.,Minami, H.,Yasuzawa-Tanaka, K.,Kuroda, T.,Oie, S.,Daitoku, H.,Okuwaki, M.,Nagata, K.,Fukamizu, A.,Kimura, K.,Shimizu, T.,Yanagisawa, J.
Epigenetic control of rDNA loci in response to intracellular energy status
Cell(Cambridge,Mass.), 133:627-639, 2008

PubMed Abstract: Intracellular energy balance is important for cell survival. In eukaryotic cells, the most energy-consuming process is ribosome biosynthesis, which adapts to changes in intracellular energy status. However, the mechanism that links energy status and ribosome biosynthesis is largely unknown. Here, we describe eNoSC, a protein complex that senses energy status and controls rRNA transcription. eNoSC contains Nucleomethylin, which binds histone H3 dimethylated Lys9 in the rDNA locus, in a complex with SIRT1 and SUV39H1. Both SIRT1 and SUV39H1 are required for energy-dependent transcriptional repression, suggesting that a change in the NAD(+)/NADH ratio induced by reduction of energy status could activate SIRT1, leading to deacetylation of histone H3 and dimethylation at Lys9 by SUV39H1, thus establishing silent chromatin in the rDNA locus. Furthermore, eNoSC promotes restoration of energy balance by limiting rRNA transcription, thus protecting cells from energy deprivation-dependent apoptosis. These findings provide key insight into the mechanisms of energy homeostasis in cells.

PubMed: 18485871
DOI: 10.1016/j.cell.2008.03.030

Experimental method

X-RAY DIFFRACTION (2 Å)