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Cloning and characterization of the human PIM‐1 gene: A putative oncogene related to the protein kinases
Author(s) -
Meeker Timothy C.,
Nagarajan Lalitha,
arRushdi Abbas,
Croce Carlo M.
Publication year - 1987
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240350204
Subject(s) - biology , gene , microbiology and biotechnology , exon , promoter , runx1t1 , tyrosine kinase , genomic dna , gas6 , genetics , receptor tyrosine kinase , kinase , gene expression , signal transduction
The mouse PIM‐l gene has been implicated in the evolution of retrovirus‐associated mouse lymphomas. We have initiated a study of the human PIM‐1 gene because of its potential importance as a human oncogene. We have isolated genomic and cDNA clones for this gene and characterized this locus in detail. The predicted PIM‐1 protein is 313 amino acids in length. It has homology to a number of the protein kinases but does not have a transmembrane region. The amino acid corresponding to tyrosine‐416 of pp60v‐src is a tyrosine (position 198), which is consistent with the hypothesis that PIM‐1 is a tyrosine kinase rather than a serine threonine kinase. The PIM‐1 gene was found to have six exons and five introns derived from 5 kb of genomic DNA. The site of transcription initiation was localized by S1 nuclease protection studies which indicated that the mature PIM‐1 mRNA was approximately 2.7 kb in length. The promotor of this gene had no TATA or CAAT box but did have multiple GC boxes (CCGCCC) that might bind the Spl protein. The PIM‐1 gene was expressed in myeloid and B lymphoid cell lines, but not in T lymphoid and nonhemopoietic lines. This initial characterization of PIM‐1 will allow us to define its role in normal and malignant hematolymphoid differentiation.