Abstract:
:SPT5 and its binding partner SPT4 function in both positively and negatively regulating transcriptional elongation. The demonstration that SPT5 and RNA polymerase II are targets for phosphorylation by CDK9/cyclin T1 indicates that posttranslational modifications of these factors are important in regulating the elongation process. In this study, we utilized a biochemical approach to demonstrate that SPT5 was specifically associated with the protein arginine methyltransferases PRMT1 and PRMT5 and that SPT5 methylation regulated its interaction with RNA polymerase II. Specific arginine residues in SPT5 that are methylated by these enzymes were identified and demonstrated to be important in regulating its promoter association and subsequent effects on transcriptional elongation. These results suggest that methylation of SPT5 is an important posttranslational modification that is involved in regulating its transcriptional elongation properties in response to viral and cellular factors.
journal_name
Mol Celljournal_title
Molecular cellauthors
Kwak YT,Guo J,Prajapati S,Park KJ,Surabhi RM,Miller B,Gehrig P,Gaynor RBdoi
10.1016/s1097-2765(03)00101-1subject
Has Abstractpub_date
2003-04-01 00:00:00pages
1055-66issue
4eissn
1097-2765issn
1097-4164pii
S1097-2765(03)00101-1journal_volume
11pub_type
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