PMID:16281054
| Citation |
Wu, M, Reuter, M, Lilie, H, Liu, Y, Wahle, E and Song, H (2005) Structural insight into poly(A) binding and catalytic mechanism of human PARN. EMBO J. 24:4082-93 |
|---|---|
| Abstract |
Poly(A)-specific ribonuclease (PARN) is a processive, poly(A)-specific 3' exoribonuclease. The crystal structure of C-terminal truncated human PARN determined in two states (free and RNA-bound forms) reveals that PARNn is folded into two domains, an R3H domain and a nuclease domain similar to those of Pop2p and epsilon186. The high similarity of the active site structures of PARNn and epsilon186 suggests that they may have a similar catalytic mechanism. PARNn forms a tight homodimer, with the R3H domain of one subunit partially enclosing the active site of the other subunit and poly(A) bound in a deep cavity of its nuclease domain in a sequence-nonspecific manner. The R3H domain and, possibly, the cap-binding domain are involved in poly(A) binding but these domains alone do not appear to contribute to poly(A) specificity. Mutations disrupting dimerization abolish both the enzymatic and RNA-binding activities, suggesting that the PARN dimer is a structural and functional unit. The cap-binding domain may act in concert with the R3H domain to amplify the processivity of PARN. |
| Links |
PubMed PMC1356309 Online version:10.1038/sj.emboj.7600869 |
| Keywords |
Adenosine/metabolism; Amino Acid Sequence; Catalytic Domain; Crystallography, X-Ray; Dimerization; Exoribonucleases/chemistry; Exoribonucleases/metabolism; Humans; Molecular Sequence Data; Polymers/metabolism; Protein Binding; Protein Structure, Tertiary; Sequence Alignment; Structural Homology, Protein |
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