P01-021 DNA methylation in vertebrate cells marks out functionally specialized regions of the genome and is strongly associated with transcriptional repression. Highly conserved DNA-binding proteins (containing methyl-CpG binding domain, MBD) has been identified and share high specificity in recognizing methylated DNA. In A. thaliana several members of the MBD family have been characterized, showing similarities to animal MBDs. Only few of them can recognize methylated DNA and their physiological and functional significance is still unclear. To study the role of AtMBD7, the only one bearing three MBD domains, we identified AtPRMT11, an arginine methyltransferase, among the protein partners. Our experiments confirmed that these two proteins interact in vitro and can be isolated together in the same complex. Analyses revealed that AtPRMT11 methylates arginines in an asymmetrical fashion and is active both on histones and cellular proteins. These data reveal for the first time in plants the direct interaction between one member of the MBD family and an arginine methyltransferase, analogously to animals where MBD2 is able to interact with and is modulated by the PRMT5 enzyme (Tan and Nakielny, 2006). Moreover we found that AtPRMT11 can methylate one of the DNA binding domains in AtMBD7 thus suggesting that AtMBD7 might act as a bridge between two global epigenetic mechanisms of gene regulation in plants. Data describing these particular interaction will be presented and discussed.
DNA and arginine methylation in Arabidopsis: the relationship between AtMBD7 and AtPRMT11
DE BASTIANI, Morena;BERNACCHIA, Giovanni
2008
Abstract
P01-021 DNA methylation in vertebrate cells marks out functionally specialized regions of the genome and is strongly associated with transcriptional repression. Highly conserved DNA-binding proteins (containing methyl-CpG binding domain, MBD) has been identified and share high specificity in recognizing methylated DNA. In A. thaliana several members of the MBD family have been characterized, showing similarities to animal MBDs. Only few of them can recognize methylated DNA and their physiological and functional significance is still unclear. To study the role of AtMBD7, the only one bearing three MBD domains, we identified AtPRMT11, an arginine methyltransferase, among the protein partners. Our experiments confirmed that these two proteins interact in vitro and can be isolated together in the same complex. Analyses revealed that AtPRMT11 methylates arginines in an asymmetrical fashion and is active both on histones and cellular proteins. These data reveal for the first time in plants the direct interaction between one member of the MBD family and an arginine methyltransferase, analogously to animals where MBD2 is able to interact with and is modulated by the PRMT5 enzyme (Tan and Nakielny, 2006). Moreover we found that AtPRMT11 can methylate one of the DNA binding domains in AtMBD7 thus suggesting that AtMBD7 might act as a bridge between two global epigenetic mechanisms of gene regulation in plants. Data describing these particular interaction will be presented and discussed.I documenti in SFERA sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
