HMT1/YBR034C Literature Guide Help

Other names published for HMT1: HCP1, ODP1, RMT1, YBR034C

HMT1 - Strains/Constructs (29)

ReferenceOther Genes Addressed
Jackson CA, et al.  (2012) Proteomic analysis of interactors for yeast protein arginine methyltransferase Hmt1 reveals novel substrate and insights into additional biological roles. Proteomics 12(22):3304-14
Milliman EJ, et al.  (2012) Recruitment of rpd3 to the telomere depends on the protein arginine methyltransferase hmt1. PLoS One 7(8):e44656
Edwards CR, et al.  (2011) Histone H4 lysine 20 of Saccharomyces cerevisiae is monomethylated and functions in subtelomeric silencing. Biochemistry 50(48):10473-83
Kerr SC, et al.  (2011) The ccr4-not complex interacts with the mRNA export machinery. PLoS One 6(3):e18302
Chen YC, et al.  (2010) Protein Arginine Methylation Facilitates Cotranscriptional Recruitment of Pre-mRNA Splicing Factors. Mol Cell Biol 30(21):5245-56
Lipson RS, et al.  (2010) Two novel methyltransferases acting upon eukaryotic elongation factor 1A in Saccharomyces cerevisiae. Arch Biochem Biophys 500(2):137-143
Webb KJ, et al.  (2010) Identification of protein N-terminal methyltransferases in yeast and humans. Biochemistry 49(25):5225-35
Estrella LA, et al.  (2009) The shuttling protein Npl3 promotes translation termination accuracy in Saccharomyces cerevisiae. J Mol Biol 394(3):410-22
Kuo MH, et al.  (2009) Functional connection between histone acetyltransferase Gcn5p and methyltransferase Hmt1p. Biochim Biophys Acta 1789(5):395-402
Sayegh J and Clarke SG  (2008) Hsl7 is a substrate-specific type II protein arginine methyltransferase in yeast. Biochem Biophys Res Commun 372(4):811-5
Hsieh CH, et al.  (2007) Expression of proteins with dimethylarginines in Escherichia coli for protein-protein interaction studies. Protein Sci 16(5):919-28
McBride AE, et al.  (2007) Protein arginine methylation in Candida albicans: role in nuclear transport. Eukaryot Cell 6(7):1119-29
Miranda TB, et al.  (2006) Yeast Hsl7 (histone synthetic lethal 7) catalyses the in vitro formation of omega-N(G)-monomethylarginine in calf thymus histone H2A. Biochem J 395(3):563-70
McBride AE, et al.  (2005) Arginine methylation of yeast mRNA-binding protein Npl3 directly affects its function, nuclear export, and intranuclear protein interactions. J Biol Chem 280(35):30888-98
Yu MC, et al.  (2004) Arginine methyltransferase affects interactions and recruitment of mRNA processing and export factors. Genes Dev 18(16):2024-35
Xu C, et al.  (2003) In vivo analysis of nucleolar proteins modified by the yeast arginine methyltransferase Hmt1/Rmt1p. RNA 9(6):746-59
Lin Q, et al.  (2001) Design of allele-specific protein methyltransferase inhibitors. J Am Chem Soc 123(47):11608-13
McBride AE, et al.  (2000) Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions. J Biol Chem 275(5):3128-36
Weiss VH, et al.  (2000) The structure and oligomerization of the yeast arginine methyltransferase, Hmt1. Nat Struct Biol 7(12):1165-71
Yun CY and Fu XD  (2000) Conserved SR protein kinase functions in nuclear import and its action is counteracted by arginine methylation in Saccharomyces cerevisiae. J Cell Biol 150(4):707-18
Valentini SR, et al.  (1999) Arginine methylation and binding of Hrp1p to the efficiency element for mRNA 3'-end formation. RNA 5(2):272-80
Li C, et al.  (1998) Protein N-arginine methylation in adenosine dialdehyde-treated lymphoblastoid cells. Arch Biochem Biophys 351(1):53-9
Scott HS, et al.  (1998) Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2). Genomics 48(3):330-40
Shen EC, et al.  (1998) Arginine methylation facilitates the nuclear export of hnRNP proteins. Genes Dev 12(5):679-91
Tang J, et al.  (1998) PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. J Biol Chem 273(27):16935-45
Zobel-Thropp P, et al.  (1998) delta-N-methylarginine is a novel posttranslational modification of arginine residues in yeast proteins. J Biol Chem 273(45):29283-6
Gary JD, et al.  (1996) The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae. J Biol Chem 271(21):12585-94
Henry MF and Silver PA  (1996) A novel methyltransferase (Hmt1p) modifies poly(A)+-RNA-binding proteins. Mol Cell Biol 16(7):3668-78
Lin WJ, et al.  (1996) The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase. J Biol Chem 271(25):15034-44