| Literature DB >> 21362551 |
Yasutake Katoh1, Tsuyoshi Ikura, Yutaka Hoshikawa, Satoshi Tashiro, Takashi Ito, Mineto Ohta, Yohei Kera, Tetsuo Noda, Kazuhiko Igarashi.
Abstract
Protein methylation pathways comprise methionine adenosyltransferase (MAT), which produces S-adenosylmethionine (SAM) and SAM-dependent substrate-specific methyltransferases. However, the function of MAT in the nucleus is largely unknown. MafK represses or activates expression of heme oxygenase-1 (HO-1) gene, depending on its heterodimer partners. Proteomics analysis of MafK revealed its interaction with MATIIα, a MAT isozyme. MATIIα was localized in nuclei and found to form a dense network with chromatin-related proteins including Swi/Snf and NuRD complexes. MATIIα was recruited to Maf recognition element (MARE) at HO-1 gene. When MATIIα was knocked down in murine hepatoma cell line, expression of HO-1 was derepressed at both basal and induced levels. The catalytic activity of MATIIα, as well as its interacting factors such as MATIIβ, BAF53a, CHD4, and PARP1, was required for HO-1 repression. MATII serves as a transcriptional corepressor of MafK by interacting with chromatin regulators and supplying SAM for methyltransferases.Entities:
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Year: 2011 PMID： 21362551 DOI： 10.1016/j.molcel.2011.02.018
Source DB: PubMed Journal: Mol Cell ISSN： 1097-2765 Impact factor: 17.970