Abstract:
:Tpt1 is an essential agent of fungal tRNA splicing that removes the 2'-PO4 at the splice junction generated by fungal tRNA ligase. Tpt1 catalyzes a unique two-step reaction whereby the 2'-PO4 attacks NAD+ to form an RNA-2'-phospho-ADP-ribosyl intermediate that undergoes transesterification to yield 2'-OH RNA and ADP-ribose-1″,2″-cyclic phosphate products. Because Tpt1 is inessential in exemplary bacterial and mammalian taxa, Tpt1 is seen as an attractive antifungal target. Here we report a 1.4 Å crystal structure of Tpt1 in a product-mimetic complex with ADP-ribose-1″-phosphate in the NAD+ site and pAp in the RNA site. The structure reveals how Tpt1 recognizes a 2'-PO4 RNA splice junction and the mechanism of RNA phospho-ADP-ribosylation. This study also provides evidence that a bacterium has an endogenous phosphorylated substrate with which Tpt1 reacts.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Banerjee A,Munir A,Abdullahu L,Damha MJ,Goldgur Y,Shuman Sdoi
10.1038/s41467-018-08211-9subject
Has Abstractpub_date
2019-01-15 00:00:00pages
218issue
1issn
2041-1723pii
10.1038/s41467-018-08211-9journal_volume
10pub_type
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