| Experimental evolution reveals a general role for the Hmt1 in heterogeneity noise buffering. | Experimental evolution reveals a general role for the methyltransferase Hmt1 in noise buffering.
You ST, Jhou YT, Kao CF, Leu JY., Free PMC Article | 02/29/2020 |
| this is the first study to reveal an association between Hmt1p and phosphate homeostasis and one which suggests a regulatory link between S-adenosyl methionine and intracellular phosphate | Knockout of the Hmt1p Arginine Methyltransferase in Saccharomyces cerevisiae Leads to the Dysregulation of Phosphate-associated Genes and Processes.
Chia SZ, Lai YW, Yagoub D, Lev S, Hamey JJ, Pang CNI, Desmarini D, Chen Z, Djordjevic JT, Erce MA, Hart-Smith G, Wilkins MR., Free PMC Article | 11/2/2019 |
| This study investigated the enzyme-substrate interaction between Hmt1p and nucleolar protein Npl3p, using chemical cross linking/mass spectrometry. This method can capture transient interprotein interactions that occur during the process of methylation, involving a disordered region in Npl3p with tandem SRGG repeats, and we confirm that Hmt1p and Npl3p exist as homomultimers. | Characterization of the Interaction between Arginine Methyltransferase Hmt1 and Its Substrate Npl3: Use of Multiple Cross-Linkers, Mass Spectrometric Approaches, and Software Platforms.
Smith DL, Götze M, Bartolec TK, Hart-Smith G, Wilkins MR. | 04/6/2019 |
| Data suggest that Hmt1-based arginine methylation is required for Scd6 localization and function. | Analysis of the Physiological Activities of Scd6 through Its Interaction with Hmt1.
Lien PT, Izumikawa K, Muroi K, Irie K, Suda Y, Irie K., Free PMC Article | 06/24/2017 |
| Arginine methylation is a widespread modification, with Hmt1 being the major arginine methyltransferase in S. cerevisiae. | Protein substrates of the arginine methyltransferase Hmt1 identified by proteome arrays.
Low JK, Im H, Erce MA, Hart-Smith G, Snyder MP, Wilkins MR. | 10/29/2016 |
| Studied and discovered 21 native sites of arginine methylation on five putative Hmt1 substrate proteins (Gar1p, Nop1p, Npl3p, Nsr1p, Rps2p). | Yeast proteins Gar1p, Nop1p, Npl3p, Nsr1p, and Rps2p are natively methylated and are substrates of the arginine methyltransferase Hmt1p.
Yagoub D, Hart-Smith G, Moecking J, Erce MA, Wilkins MR. | 06/28/2016 |
| the methyltransferase activity of Hmt1 on histone H3R2 requires reciprocal contributions from two Hmt1 molecules, suggesting an intermolecular trans-complementary mechanism by which Hmt1 dimer methylates its substrates | Yeast Hmt1 catalyses asymmetric dimethylation of histone H3 arginine 2 in vitro.
Li HT, Gong T, Zhou Z, Liu YT, Cao X, He Y, Chen CD, Zhou JQ. | 06/27/2015 |
| Carried out a proteomic profiling experiment to comprehensively identify the physical interactors of Hmt1, the budding yeast homolog for human PRMT1. Snf2 was experimentally confirmed as a robust substrate of Hmt1 in vitro. | Proteomic analysis of interactors for yeast protein arginine methyltransferase Hmt1 reveals novel substrate and insights into additional biological roles.
Jackson CA, Yadav N, Min S, Li J, Milliman EJ, Qu J, Chen YC, Yu MC. | 05/11/2013 |
| Interactions between HMT1 and genes encoding components of the histone deacetylase complex Rpd3L, are reported. | Recruitment of Rpd3 to the telomere depends on the protein arginine methyltransferase Hmt1.
Milliman EJ, Yadav N, Chen YC, Muddukrishna B, Karunanithi S, Yu MC., Free PMC Article | 02/9/2013 |
| These results are suggestive of a role for Rmt1 in modifying the function of Rps2 in a manner distinct from that occurring in S. pombe and mammalian cells. | Rmt1 catalyzes zinc-finger independent arginine methylation of ribosomal protein Rps2 in Saccharomyces cerevisiae.
Lipson RS, Webb KJ, Clarke SG., Free PMC Article | 03/8/2010 |
| Results reveal a functional connection between histone acetylation, methylation, and two of the responsible enzymes, Gcn5p and Hmt1p. | Functional connection between histone acetyltransferase Gcn5p and methyltransferase Hmt1p.
Kuo MH, Xu XJ, Bolck HA, Guo D., Free PMC Article | 01/21/2010 |
| Loss of Hmt1's catalytic activity results in dimethylated Arg-3 histone H4 occupancy across silent chromatin regions. | The role of protein arginine methylation in the formation of silent chromatin.
Yu MC, Lamming DW, Eskin JA, Sinclair DA, Silver PA., Free PMC Article | 01/21/2010 |