Linked Life Data

7490087

Source:http://linkedlifedata.com/resource/pubmed/id/7490087

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-1-3
pubmed:databankReference
pubmed:abstractText
Protein tyrosine phosphatases comprise a large family of enzymes that are involved in the control of cellular tyrosine phosphorylation. We have used lambda phage analysis to elucidate the complete genomic structure of an intracellular member of this family, the murine MPTP-PEST gene. Eight overlapping lambda phage clones representing the MPTP-PEST locus were isolated from a 129/sv mouse genomic library. The gene spans over 90 kb of the mouse genome and is composed of 18 exons, 10 of which constitute the catalytic phosphatase domain. Detailed comparison of the position of intron/exon boundaries of the phosphatase domain of MPTP-PEST to those of several other protein tyrosine phosphatases indicates that the MPTP-PEST catalytic domain contains additional exons as a consequence of the insertion of novel introns. In addition, this analysis reveals a strong conservation of the genomic organization within the catalytic domain of the protein tyrosine phosphatase gene family. Finally, fluorescence in situ hybridization with MPTP-PEST genomic DNA refines the map position of MPTP-PEST to mouse chromosome 5A3 to B. This result is in agreement with the previous mapping of the human PEST gene to chromosome 7q11.23, a region of synteny with the centromeric portion of mouse chromosome 5.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0888-7543
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
501-7
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Structure of the murine MPTP-PEST gene: genomic organization and chromosomal mapping.
pubmed:affiliation
Department of Biochemistry, McGill University, Montreal, Quebec, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't