How an RNA ligase discriminates RNA versus DNA damage Journal Article


Authors: Nandakumar, J.; Shuman, S.
Article Title: How an RNA ligase discriminates RNA versus DNA damage
Abstract: T4 RNA ligase 2 (Rnl2) exemplifies a family of RNA-joining enzymes that includes protozoan RNA-editing ligases. Rnl2 efficiently seals 3′-OH/5′-PO4 RNA nicks in either a duplex RNA or an RNA:DNA hybrid but cannot seal DNA nicks. RNA specificity arises from a requirement for at least two ribonucleotides immediately flanking the 3′-OH of the nick; the rest of the nicked duplex can be replaced by DNA. The terminal 2′-OH at the nick is important for the attack of the 3′-OH on the 5′-adenylated strand to form a phosphodiester, but dispensable for nick recognition and adenylylation of the 5′-PO 4 strand. The penultimate 2′-OH is important for nick recognition. Stable binding of Rnl2 at a nick depends on contacts to both the N-terminal adenylyltransferase domain and its signature C-terminal domain. Nick sensing also requires adenylylation of Rnl2. These results provide insights to the evolution of nucleic acid repair systems.
Keywords: dna damage; rna; dna; amino terminal sequence; substrate specificity; nick end labeling; protozoa; rna ligase (atp); rna binding; viral proteins; adenylation; ribonucleotide; dna strand; ribonucleotides; rna ligase; rna hybridization; bacteriophage t4; oligoribonucleotide; phocidae; article; dna hybrid; oligodeoxyribonucleotide
Journal Title: Molecular Cell
Volume: 16
Issue: 2
ISSN: 1097-2765
Publisher: Cell Press  
Date Published: 2004-10-22
Start Page: 211
End Page: 221
Language: English
DOI: 10.1016/j.molcel.2004.09.022
PROVIDER: scopus
PUBMED: 15494308
DOI/URL:
Notes: Mol. Cell -- Cited By (since 1996):36 -- Export Date: 16 June 2014 -- CODEN: MOCEF -- Source: Scopus
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  1. Stewart H Shuman
    546 Shuman