Linked Life Data

8579355

Source:http://linkedlifedata.com/resource/pubmed/id/8579355

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-3-8
pubmed:databankReference
pubmed:abstractText
Eukaryotes synthesize queuosine (nucleoside Q) by the irreversible base-for-base exchange of queuine (Q base) for guanine at tRNA position 34, a reaction catalyzed by tRNA-guanine transglycosylase (TGT). The physiological role of Q remains unknown but the tRNA of tumor cells often is undermodified with respect to Q. Toward an understanding of the function of Q in normal and neoplastic cells we have isolated and characterized the cDNA for rabbit TGT. Rabbit erythrocyte TGT was reported previously to be a dimer of 60- and 43-kDa subunits (N. K. Howes and W. R. Farkas, 1978, J. Biol. Chem. 253, 9082-9078). Here we present the cDNA sequence for the apparent 60-kDa subunit; it contains an open reading frame encoding a 493-residue protein. The rabbit TGT 60-kDa subunit shares significant sequence similarity with the deubiquitinating enzyme family (F. R. Papa and M. Hochstrasser, 1993, nature 366, 313-319), especially with sequence elements that include conserved Cys and His residues.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
326
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Cloning and characterization of cDNA encoding the rabbit tRNA-guanine transglycosylase 60-kilodalton subunit.
pubmed:affiliation
Department of Microbiology and Immunology, University of Tennessee, Memphis 38163, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't