The C-terminal domain of T4 RNA ligase 1 confers specificity for tRNA repair Journal Article

   

Authors:	Wang, L. K.; Nandakumar, J.; Schwer, B.; Shuman, S.
Article Title:	The C-terminal domain of T4 RNA ligase 1 confers specificity for tRNA repair
Abstract:	T4 RNA ligase 1 (Rnl1) is a tRNA repair enzyme that thwarts a tRNA-damaging host response to virus infection. The 374-aa Rnl1 protein consists of an N-terminal nucleotidyltransferase domain fused to a unique C-terminal domain composed of 10 α helices. We exploited an in vitro tRNA splicing system to demonstrate that Rnl1 has an inherent specificity for sealing tRNA with a break in the anticodon loop. The tRNA specificity is imparted by the C domain, any deletion of which caused the broken tRNA to be sealed as poorly as the linear intron in vitro and also abolished Rnl1 tRNA splicing activity in vivo. Deletion analysis demarcated Rnl1-(1-254) as a minimal catalytic domain of Rnl1, capable of all chemical steps of the nonspecific RNA ligation reaction. Alanine scanning of the N domain identified Ser103, Leu104, Lys117, and Ser118 as important for pRNA ligation in vitro and tRNA repair in vivo. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 RNA Society.
Keywords:	controlled study; gene deletion; nonhuman; genetic analysis; serine; carboxy terminal sequence; intron; in vitro study; dna strand breakage; amino acid sequence; molecular sequence data; sequence alignment; models, molecular; protein structure, tertiary; alanine; transfer rna; rna, transfer; leucine; trna splicing; lysine; rna ligase (atp); anticodon; rna splicing; viral proteins; enzyme active site; rna repair; rna ligase; polynucleotide ligase; trna breakage; bacteriophage t4
Journal Title:	RNA
Volume:	13
Issue:	8
ISSN:	1355-8382
Publisher:	Cold Spring Harbor Laboratory Press
Date Published:	2007-08-01
Start Page:	1235
End Page:	1244
Language:	English
DOI:	10.1261/rna.591807
PUBMED:	17585047
PROVIDER:	scopus
PMCID:	PMC1924901
DOI/URL:	http://www.scopus.com/inward/record.url?eid=2-s2.0-34447544190&partnerID=40&md5=52e24b352e65d84d15c8578e77b46a81
Notes:	--- - "Cited By (since 1996): 5" - "Export Date: 17 November 2011" - "CODEN: RNARF" - "Source: Scopus"

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