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Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3)
- 1.0371328 - MBÚ 2012 RIV NL eng J - Journal Article
Handrková, H. - Petrák, J. - Halada, Petr - Pospíšilová, D. - Čmejla, R.
Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3).
Biochimica Et Biophysica Acta-Proteins and Proteomics. Roč. 1814, č. 2 (2011), s. 277-282. ISSN 1570-9639. E-ISSN 1878-1454
R&D Projects: GA MŠMT LC07017
Institutional research plan: CEZ:AV0Z50200510
Keywords : DIAMOND-BLACKFAN ANEMIA * SUBSTRATE-SPECIFICITY * N-METHYLTRANSFERASE
Subject RIV: CE - Biochemistry
Impact factor: 3.635, year: 2011
Protein arginine methyltransferase 3 (PRMT3) is a cytosolic enzyme that catalyzes the formation of mono- and asymmetric dimethyl arginines, with ribosomal protein (RP) S2 as its main in vivo substrate. The interplay of PRMT3-RPS2 homologs in yeast is important for regulating the ribosomal subunit ratio and assembly. Prmt3–null mice display slower embryonic growth and development, although this phenotype is milder than in mouse RP gene knockouts. Defects in ribosome maturation are the hallmark of Diamond-Blackfan anemia (DBA). Sequencing of the PRMT3 gene in patients from the Czech DBA registry revealed a heterozygous mutation encoding the Tyr87Cys substitution
Permanent Link: http://hdl.handle.net/11104/0204869
Number of the records: 1