DAZAP1 interacts via its RNA-recognition motifs with the C-termini of other RNA-binding proteins.
The turnover and translation of many human mRNAs is regulated by AU-rich elements present in their 3?untranslated region, which bind various trans acting factors. We previously identified a trans acting factor that interacts with these cis elements as DAZAP1 (deleted in Azoospermia (DAZ)-Associated Protein 1), whose interaction with the germ cell-specific protein DAZ was disrupted by the phosphorylation of DAZAP1. Here we have identified several other RNA-binding proteins as binding partners for DAZAP1 in non-germinal cells. Unlike DAZ, these interactions occur between the RNA recognition motifs of DAZAP1 and the C-termini of the binding partners and in a phosphorylation-independent manner. The results suggest that DAZAP1 is a component of complexes that are crucial for the degradation and silencing of mRNA.
Yang
Huei-Ting
HT
MRC Protein Phosphorylation Unit, Sir James Black Centre, University of Dundee, Dow Street, Dundee, DD1 5EH, United Kingdom.
Peggie
Mark
M
Cohen
Philip
P
Rousseau
Simon
S
D020816:Amino Acid Motifs; D002460:Cell Line; D020868:Gene Silencing; D034441:Heterogeneous-Nuclear Ribonucleoproteins / Q000378:metabolism*; D006801:Humans; D012333:RNA, Messenger / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D020798:Two-Hybrid System Techniques
C412481:DAZAP1 protein, human; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D012333:RNA, Messenger; D016601:RNA-Binding Proteins