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Title 

PRMT3 inhibits ubiquitination of ribosomal protein S2 and together forms an active enzyme complex

Authors 

See Young ChoiCho-Rok JungJ Y KimDong Soo Im

Publisher 

Elsevier

Issue Date 

2008

Citation 

Biochimica et Biophysica Acta (BBA) - General Subjects, vol. 1780, no. 9, pp. 1062-1069

Keywords 

arginine methylationPRMT3ribosomal protein S2ubiquitin-proteasomeribosomal protein s2ribosome proteinubiquitinationenzyme activityprotein bindingrecombinant fusion proteins

Abstract 

Protein arginine methyltransferase 3 (PRMT3) comprises a region not required for catalytic activity in its amino-terminus and the core domain catalyzing protein arginine methylation. PRMT3 has been shown to interact with the 40S ribosomal protein S2 (rpS2) and methylate arginine residues in the arginine-glycine (RG) repeat region in the amino-terminus of rpS2. We investigated the biological implications of this interaction by delineating the domains that mediate binding between PRMT3 and rpS2. The rpS2 (100-293 amino acids) domain, but not the amino-terminus of rpS2 that includes the RG repeat region was essential for binding to PRMT3 and was susceptible to degradation. The amino-terminus of PRMT3, but not its catalytic core was required for binding to and the stability of rpS2. Overexpressed rpS2 was ubiquitinated in cells, but expression of PRMT3 reduced this ubiquitination and stabilized the rpS2 protein. Recombinant PRMT3 formed an active enzyme complex with endogenous rpS2 in vitro. Recombinant rpS2 in molar excess modestly increased the enzymatic activity of PRMT3 in vitro. Our results suggest that in addition to its catalytic function, PRMT3 may control the level of rpS2 protein in cells by inhibiting ubiquitin-mediated proteolysis of rpS2, while rpS2 may regulate the enzymatic activity of PRMT3 as a likely non-catalytic subunit.

ISSN 

0304-4165

Link 

http://dx.doi.org/10.1016/j.bbagen.2008.05.010

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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