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PMID:11756452

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Citation

Friesen, WJ, Wyce, A, Paushkin, S, Abel, L, Rappsilber, J, Mann, M and Dreyfuss, G (2002) A novel WD repeat protein component of the methylosome binds Sm proteins. J. Biol. Chem. 277:8243-7

Abstract

We have recently described a large (20 S) protein arginine methyltransferase complex, termed the methylosome, that contains the methyltransferase JBP1 (PRMT5) and the pICln protein. The methylosome functions to modify specific arginines to dimethylarginines in the arginine- and glycine-rich domains of several spliceosomal Sm proteins, and this modification targets these proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein (snRNP) core particles. Here, we describe a novel component of the methylosome, a 50-kilodalton WD repeat protein termed methylosome protein 50 (MEP50). We show that MEP50 is important for methylosome activity and binds to JBP1 and to a subset of Sm proteins. Because WD repeat proteins provide a platform for multiple protein interactions, MEP50 may function to mediate the interaction of multiple substrates with the methylosome. Interestingly, all of the known components of the methylosome bind Sm proteins, suggesting that in addition to producing properly methylated substrates for the SMN complex, the methylosome may be involved in Sm protein rearrangements or pre-assembly required for snRNP biogenesis.

Links

PubMed Online version:10.1074/jbc.M109984200

Keywords

Adaptor Proteins, Signal Transducing; Amino Acid Sequence; Arginine/chemistry; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Centrifugation, Density Gradient; DNA/metabolism; Electrophoresis, Polyacrylamide Gel; Glutathione Transferase/metabolism; HeLa Cells; Humans; Immunoblotting; Methylation; Molecular Sequence Data; Plasmids/metabolism; Protein Binding; Protein Methyltransferases/metabolism; Protein Structure, Tertiary; Protein-Arginine N-Methyltransferases/chemistry; Repetitive Sequences, Amino Acid; Ribonucleoproteins, Small Nuclear/chemistry; Ribonucleoproteins, Small Nuclear/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:ANM5

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P54105

F

Seeded From UniProt

complete

HUMAN:ANM5

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q9BQA1

F

Seeded From UniProt

complete

HUMAN:ICLN

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:O14744

F

Seeded From UniProt

complete

HUMAN:MEP50

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:O14744

F

Seeded From UniProt

complete

HUMAN:ANM5

enables

GO:0042802: identical protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:O14744

F

Seeded From UniProt

complete


See also

References

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