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Structures of the PIN domains of SMG6 and SMG5 reveal a nuclease within the mRNA surveillance complex

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Behm-Ansmant,  I
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Izaurralde,  E
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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引用

Glavan, F., Behm-Ansmant, I., Izaurralde, E., & Conti, E. (2006). Structures of the PIN domains of SMG6 and SMG5 reveal a nuclease within the mRNA surveillance complex. EMBO Journal, 25(21), 5117-5125. doi:10.1038/sj.emboj.7601377.


引用: https://hdl.handle.net/21.11116/0000-000A-6079-2
要旨
SMG6 and SMG5 are essential factors in nonsense-mediated mRNA decay, a conserved pathway that degrades mRNAs with premature translation termination codons. Both SMG5 and SMG6 have been predicted to contain a C-terminal PIN (PilT N-terminus) domain, present in proteins with ribonuclease activity. We have determined the structures of human SMG5 and SMG6 PIN domains. Although they share a similar overall fold related to ribonucleases of the RNase H family, they have local differences at the putative active site. SMG6 has the canonical triad of acidic residues that are crucial in RNase H for nuclease activity, while SMG5 lacks key catalytic residues. The structural differences are reflected at the functional level. Only the PIN domain of SMG6 has degradation activity on single-stranded RNA in vitro. This difference in catalytic activity is conserved in Drosophila, where an SMG6 with an inactive PIN domain inhibits NMD in a dominant-negative manner. Our findings suggest that the NMD machinery has intrinsic nuclease activity that is likely to contribute to the rapid decay of mRNAs that terminate translation prematurely.