https://scholars.lib.ntu.edu.tw/handle/123456789/407568
標題: | Effect of lysine methylation and acetylation on the RNA recognition and cellular uptake of Tat-derived peptides | 作者: | Liu, M.-C. Chen, C.-Y. Chiang, C.-H. Wang, W.-M. Cheng, R.P |
關鍵字: | Acetylation; Cellular uptake; Lysine; Methylation; RNA recognition; Tat-derived peptide | 公開日期: | 2016 | 卷: | 24 | 期: | 21 | 起(迄)頁: | 5047-5051 | 來源出版物: | Bioorganic and Medicinal Chemistry | 摘要: | The two lysine (Lys) residues in the human immunodeficiency virus trans-activator of transcription protein (HIV Tat protein) basic region (residues 47–57) are crucial for two bioactivities: RNA recognition and cellular uptake. Since the post-translational modifications of these two Lys residues affect the biological function of the Tat protein, we investigated the effect of methylation and acetylation of Lys50 and Lys51 in Tat-derived peptides on the two bioactivities. Tat-derived peptides, in which each lysine was replaced with a methylated- or acetylated-Lys, were synthesized by solid phase peptide synthesis. TAR RNA recognition of the peptides was studied by electrophoretic mobility shift assays. Cellular uptake of the peptides into Jurkat cells was determined by flow cytometry. Our results showed that acetylation of either Lys residue attenuated both bioactivities. In contrast, the effect of Lys methylation on the bioactivities depended on position and number of methyl groups. These findings should be useful for the development of functional molecules containing ammonium groups for RNA recognition to affect biological processes and for cellular uptake for drug delivery. ? 2016 Elsevier Ltd |
URI: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84991510864&doi=10.1016%2fj.bmc.2016.08.015&partnerID=40&md5=115740059f7d10900e8abcbe49a3f5b3 https://scholars.lib.ntu.edu.tw/handle/123456789/407568 |
DOI: | 10.1016/j.bmc.2016.08.015 | SDG/關鍵字: | ammonia; lysine; transactivator protein; lysine; peptide; transactivator protein; virus RNA; Article; controlled study; drug delivery system; enzyme activity; flow cytometry; gel mobility shift assay; jurkat cell line; limit of quantitation; nonhuman; protein acetylation; protein methylation; protein processing; protein synthesis; RNA analysis; RNA binding; RNA recognition; acetylation; chemistry; human; hydrogen bond; Jurkat cell line; metabolism; methylation; synthesis; Acetylation; Humans; Hydrogen Bonding; Jurkat Cells; Lysine; Methylation; Peptides; RNA, Viral; tat Gene Products, Human Immunodeficiency Virus |
顯示於: | 化學系 |
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