Increased lysine N-methylation of a 23-kDa protein during hepatic regeneration
| Autor: | Moon-Kee Paik, Yong-Bock Choi, Kyeong-Man Hong, Dong-Eun Park, Chang-Ho Shin, Kyung Suk Kim, Myoung-Hyun Ko |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Methyltransferase
Arginine Clinical Biochemistry Lysine Biology Methylation Biochemistry Histones Rats Sprague-Dawley Animals Hepatectomy Nuclear protein Molecular Biology Ammonium sulfate precipitation chemistry.chemical_classification DNA Helicases Cytochromes c Proteins Histone-Lysine N-Methyltransferase Molecular biology Liver regeneration Liver Regeneration Rats Amino acid Liver chemistry Molecular Medicine |
| Zdroj: | Experimental & Molecular Medicine. 37:155-160 |
| ISSN: | 2092-6413 |
| DOI: | 10.1038/emm.2005.21 |
| Popis: | The methylation of a 23-kDa nuclear protein increased after partial hepatectomy and methylation returned to basal levels after the initial stage of regeneration. The methylating enzyme was partially purified from rat liver by ammonium sulfate precipitation, DEAE-anion exchange chromatography and Butyl-Sepharose chromatography. The 23-kDa protein was purified from a nuclear fraction of liver tissue with SP-Sepharose. When the 23-kDa protein was methylated with the partially purified methyltransferase and analyzed on C(18) high performance liquid chromatography (HPLC), the methylated acceptor amino acid was monomethyl lysine (MML). Previously, only arginine N-methylation of specific substrate proteins has been reported during liver regeneration. However, in this report, we found that lysine N-methylation increased during early hepatic regeneration, suggesting that lysine N-methylation of the 23-kDa nuclear protein may play a functional role in hepatic regeneration. The methyltransferase did not methylate other proteins such as histones, hnRNPA1, or cytochrome C, suggesting the enzyme is a 23-kDa nuclear protein- specific lysine N-methyltransferase. |
| Databáze: | OpenAIRE |
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