@article{a91deaefd2694966b6cda0f27e736789,
title = "Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties",
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.",
author = "Kwak, {Youn Tae} and Jun Guo and Shashi Prajapati and Park, {Kyu Jin} and Surabhi, {Rama M.} and Brady Miller and Peter Gehrig and Gaynor, {Richard B.}",
note = "Funding Information: In vitro transcription reactions to assay for DRB sensitivity were carried out as described previously (Wada et al., 1998a) utilizing SPT5-immunodepleted HeLa nuclear extract (∼30 μg), 250 ng of circular pTF3-6C2AT template with a 380 bp G-less cassette, and 10 μl of purified SPT4 and either wild-type or the mutant SPT5 proteins. In vitro transcription analysis of the HIV-1 LTR was performed in the presence and absence of Tat with 100 ng of circular templates containing either wild-type HIV-1 sequences (+454 to +1092) or similar HIV-1 sequences with a mutation in the TAR RNA loop sequences between +31 and +34 (Wu-Baer et al., 1998) . Following gel electrophoresis, the gels were dried and subjected to autoradiography, and the assays were quantitated by a ChemiImager 4400. We thank Sharon Johnson for preparing the manuscript and Alex Herrera for assistance with the figures. PRMT1, PRMT3, PRMT4, and PRMT5 cDNAs were the kind gifts of Steve Clarke and Dongsoo Im, respectively. This work was supported by a grant from the Robert Welch Foundation and the NIH. ",
year = "2003",
month = apr,
day = "1",
doi = "10.1016/S1097-2765(03)00101-1",
language = "English (US)",
volume = "11",
pages = "1055--1066",
journal = "Molecular cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "4",
}