Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3)

0371328 - MBÚ 2012 RIV NL eng J - Článek v odborném periodiku
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
Grant CEP: GA MŠMT LC07017
Výzkumný záměr: CEZ:AV0Z50200510
Klíčová slova: DIAMOND-BLACKFAN ANEMIA * SUBSTRATE-SPECIFICITY * N-METHYLTRANSFERASE
Kód oboru RIV: CE - Biochemie
Impakt faktor: 3.635, rok: 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
Trvalý link: http://hdl.handle.net/11104/0204869