Bacterial Hen1 is a 3′ terminal RNA ribose 2′-O- methyltransferase component of a bacterial RNA repair cassette Journal Article

   

Authors:	Jain, R.; Shuman, S.
Article Title:	Bacterial Hen1 is a 3′ terminal RNA ribose 2′-O- methyltransferase component of a bacterial RNA repair cassette
Abstract:	Hen1 is an RNA ribose 2′-O-methyltransferase that modifies the 3′ terminal nucleoside of eukaryal small regulatory RNAs. Here, we report that Hen1 homologs are present in bacterial proteomes from eight different phyla. Bacterial Hen1 is encoded by the proximal ORF of a two-gene operon that also encodes polynucleotide kinase-phosphatase (Pnkp), an RNA repair enzyme. Purified recombinant Clostridium thermocellum Hen1 is a homodimer of a 465-amino acid polypeptide. CthHen1 catalyzes methyl transfer from AdoMet to the 3′ terminal nucleoside of an RNA oligonucleotide, but is unreactive with a synonymous DNA oligonucleotide or an RNA with a single 3′-terminal deoxyribose sugar. CthHen1 is optimally active at alkaline pH and dependent on manganese. Activity is inhibited by AdoHcy and abolished by mutations D291A and D316A in the putative AdoMet-binding pocket. The C-terminal fragment, Hen1-(259-465), comprises an autonomous monomeric methyltransferase domain. Copyright © 2010 RNA Society. Published by Cold Spring Harbor Laboratory Press. Copyright © 2010 RNA Society.
Keywords:	controlled study; unclassified drug; sequence analysis; nonhuman; protein domain; carboxy terminal sequence; enzyme activity; bacteria (microorganisms); methyltransferase; bacterial proteins; methyltransferases; amino acid sequence; molecular sequence data; sequence homology, amino acid; protein multimerization; adomet; eukaryota; recombinant proteins; substrate specificity; base sequence; protein structure, tertiary; catalysis; monomer; rna, bacterial; magnesium; s-adenosylmethionine; open reading frame; rna end-healing; rna repair; transmethylation; operon; s adenosylmethionine; 3' terminal rna ribose 2' o methyltransferase; protein hen1; s adenosylhomocysteine; alkalinity; clostridium thermocellum
Journal Title:	RNA
Volume:	16
Issue:	2
ISSN:	1355-8382
Publisher:	Cold Spring Harbor Laboratory Press
Date Published:	2010-02-01
Start Page:	316
End Page:	323
Language:	English
DOI:	10.1261/rna.1926510
PUBMED:	20007328
PROVIDER:	scopus
PMCID:	PMC2811661
DOI/URL:	http://www.scopus.com/inward/record.url?eid=2-s2.0-75149121115&partnerID=40&md5=bfa7ac295359453ccfa757230b9ea6d6
Notes:	--- - "Cited By (since 1996): 2" - "Export Date: 20 April 2011" - "CODEN: RNARF" - "Source: Scopus"

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