HMT1 cDNA ORF clone, Saccharomyces cerevisiae S288C

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

Complete DNA sequence of yeast chromosome II.
Feldmann H, Aigle M, Aljinovic G, Andr? B, Baclet MC, Barthe C, Baur A, B?cam AM, Biteau N, Boles E, Brandt T, Brendel M, Br?ckner M, Bussereau F, Christiansen C, Contreras R, Crouzet M, Cziepluch C, D?molis N, Delaveau T, Doignon F, Domdey H, D?sterhus S, Dubois E, Dujon B, El Bakkoury M, Entian KD, Feurmann M, Fiers W, Fobo GM, Fritz C, Gassenhuber H, Glandsdorff N, Goffeau A, Grivell LA, de Haan M, Hein C, Herbert CJ, Hollenberg CP, Holmstr?m K, Jacq C, Jacquet M, Jauniaux JC, Jonniaux JL, Kalles?e T, Kiesau P, Kirchrath L, K?tter P, Korol S, Liebl S, Logghe M, Lohan AJ, Louis EJ, Li ZY, Maat MJ, Mallet L, Mannhaupt G, Messenguy F, Miosga T, Molemans F, M?ller S, Nasr F, Obermaier B, Perea J, Pi?rard A, Piravandi E, Pohl FM, Pohl TM, Potier S, Proft M, Purnelle B, Ramezani Rad M, Rieger M, Rose M, Schaaff-Gerstenschl?ger I, Scherens B, Schwarzlose C, Skala J, Slonimski PP, Smits PH, Souciet JL, Steensma HY, Stucka R, Urrestarazu A, van der Aart QJ, van Dyck L, Vassarotti A, Vetter I, Vierendeels F, Vissers S, Wagner G, de Wergifosse P, Wolfe KH, Zagulski M, Zimmermann FK, Mewes HW, Kleine K
The EMBO journal13(24)5795-809(1994 Dec)

Arginine methylation is a widespread modification, with Hmt1 being the major arginine methyltransferase in S. cerevisiae.
Title: Protein substrates of the arginine methyltransferase Hmt1 identified by proteome arrays.

Data suggest that Hmt1-based arginine methylation is required for Scd6 localization and function.
Title: Analysis of the Physiological Activities of Scd6 through Its Interaction with Hmt1.

Studied and discovered 21 native sites of arginine methylation on five putative Hmt1 substrate proteins (Gar1p, Nop1p, Npl3p, Nsr1p, Rps2p).
Title: Yeast proteins Gar1p, Nop1p, Npl3p, Nsr1p, and Rps2p are natively methylated and are substrates of the arginine methyltransferase Hmt1p.

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
Title: Yeast Hmt1 catalyses asymmetric dimethylation of histone H3 arginine 2 in?vitro.

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.
Title: Proteomic analysis of interactors for yeast protein arginine methyltransferase Hmt1 reveals novel substrate and insights into additional biological roles.