Differential hnRNP D isoform incorporation may confer plasticity to the ESSV-mediated repressive state across HIV-1 exon 3

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• 作者：Frank Hillebrand^a ; ¹ ; Jan Otto Peter^a ; ¹ ; Anna-Lena Brillen^a ; Marianne Otte^c ; Heiner Schaal^a ; ; Steffen Erkelenz^a ; ^b ; ^{steffen.erkelenz@gmx.de}
• 关键词：HIV-1 ; Splicing ; hnRNP proteins ; hnRNP D
• 刊名：Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：1860
• 期：2
• 页码：205-217
• 全文大小：1502 K
• 卷排序：1860

文摘

The glycine-rich domain (GRD) of hnRNP proteins is a unifying feature in splice site repression. hnRNP D proteins act as splicing repressors when bound to exonic positions. hnRNP D proteins associate with the HIV-1 ESSV silencer complex. Mutual interference between hnRNP A1 and D facilitates a dynamic regulation of the repressive state of HIV-1 exon 3.