Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-10-5
pubmed:databankReference
pubmed:abstractText
Mono(ADP-ribosyl)transferases regulate the function of target proteins by attaching ADP-ribose to specific amino acid residues in their target proteins. The purpose of this study was to determine the structure, chromosomal localization, and expression profile of the gene for mouse ecto-ADP-ribosyltransferase ART5. Southern blot analyses indicate that Art5 is a single copy gene which maps to mouse chromosome 7 at offset 49.6 cM in close proximity to the Art1, Art2a and Art2b genes. Northern blot and RT-PCR analyses demonstrate prominent expression of Art5 in testis, and lower levels in cardiac and skeletal muscle. Sequence analyses reveal that the Art5 gene encompasses six exons spanning 8 kb of genomic DNA. The 5' end of the Art5 gene overlaps with that of the Art1 gene. A single long exon encodes the predicted ART5 catalytic domain. Separate exons encode the N-terminal leader peptide and a hydrophilic C-terminal extension. Sequencing of RT-PCR products and ESTs identified six splice variants. The deduced amino acid sequence of ART5 shows 87% sequence identity to its orthologue from the human, and 37 and 32% identity to its murine paralogues ART1 and ART2. Unlike ART1 and ART2, ART5 lacks a glycosylphosphatidylinositol-anchor signal sequence and is predicted to be a secretory enzyme. This prediction was confirmed by transfecting an Art5 cDNA expression construct into Sf9 insect cells. The secreted epitope-tagged ART5 protein resembled rat ART2 in exhibiting potent NAD-glycohydrolase activity. This study provides important experimental tools to further elucidate the function of ART5.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
267-77
pubmed:dateRevised
2009-9-4
pubmed:meshHeading
pubmed-meshheading:11587854-ADP Ribose Transferases, pubmed-meshheading:11587854-Amino Acid Sequence, pubmed-meshheading:11587854-Animals, pubmed-meshheading:11587854-Base Sequence, pubmed-meshheading:11587854-Blotting, Northern, pubmed-meshheading:11587854-Cell Line, pubmed-meshheading:11587854-Chromosome Mapping, pubmed-meshheading:11587854-DNA, pubmed-meshheading:11587854-DNA, Complementary, pubmed-meshheading:11587854-Exons, pubmed-meshheading:11587854-Female, pubmed-meshheading:11587854-Gene Expression, pubmed-meshheading:11587854-Genes, pubmed-meshheading:11587854-Introns, pubmed-meshheading:11587854-Isoenzymes, pubmed-meshheading:11587854-Male, pubmed-meshheading:11587854-Mice, pubmed-meshheading:11587854-Mice, Inbred BALB C, pubmed-meshheading:11587854-Mice, Inbred Strains, pubmed-meshheading:11587854-Molecular Sequence Data, pubmed-meshheading:11587854-Muridae, pubmed-meshheading:11587854-RNA, Messenger, pubmed-meshheading:11587854-Sequence Alignment, pubmed-meshheading:11587854-Sequence Analysis, DNA, pubmed-meshheading:11587854-Sequence Homology, Amino Acid, pubmed-meshheading:11587854-Tissue Distribution
pubmed:year
2001
pubmed:articleTitle
Structure, chromosomal localization, and expression of the gene for mouse ecto-mono(ADP-ribosyl)transferase ART5.
pubmed:affiliation
Institute for Immunology, University Hospital, Martinistrasse 52, 20246 Hamburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't