Structure of tRNA splicing enzyme Tpt1 illuminates the mechanism of RNA 2′-PO4 recognition and ADP-ribosylation-Reference-Cited by-同舟云学术

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Structure of tRNA splicing enzyme Tpt1 illuminates the mechanism of RNA 2′-PO4 recognition and ADP-ribosylation

Published:2019-01-15 Issue:1 Volume:10 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Banerjee Ankan,Munir Annum,Abdullahu Leonora,Damha Masad J.,Goldgur Yehuda,Shuman Stewart

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/s41467-018-08211-9.pdf

Reference31 articles.

1. Culver, G. M. et al. An NAD derivative produced during transfer RNA splicing: ADP-ribose 1″-2″ cyclic phosphate. Science 261, 206–208 (1993).

2. Spinelli, S. L., Kierzek, R., Turner, D. H. & Phizicky, E. M. Transient ADP-ribosylation of a 2′-phosphate implicated in its removal from ligated tRNA during splicing in yeast. J. Biol. Chem. 274, 2637–2644 (1999).

3. Steiger, M. A., Kierzek, R., Turner, D. H. & Phizicky, E. M. Substrate recognition by a yeast 2′-phosphotransferase involved in tRNA splicing and its Escherichia coli homolog. Biochemistry 40, 14098–14105 (2001).

4. Steiger, M. A., Jackman, J. E. & Phizicky, E. M. Analysis of 2′-phosphotransferase (Tpt1p) from Saccharomyces cerevisiae: evidence for a conserved two-step reaction mechanism. RNA 11, 99–106 (2005).

5. Munir, A., Abdullahu, L., Damha, M. J. & Shuman, S. Two-step mechanism and step-arrest mutants of Runella slithyformis NAD+-dependent tRNA 2′-phosphotransferase Tpt1. RNA 24, 1144–1157 (2018).

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1. Chemical synthesis of 2″OMeNAD+ and its deployment as an RNA 2′-phosphotransferase (Tpt1) ‘poison’ that traps the enzyme on its abortive RNA-2′-PO4-(ADP-2″OMe-ribose) reaction intermediate;Nucleic Acids Research;2024-08-20

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