Characterization of a novel murine testis-specific serine/threonine kinase

Using degenerate oligos corresponding to two highly conserved motifs within the protein kinase catalytic domain and a PCR-based cloning strategy, we have isolated a cDNA fragment encoding a new member of the Ser/Thr (serine/threonine) familiy of protein kinases. Expression analysis revealed that the...

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Veröffentlicht in:Gene 1994-02, Vol.139 (2), p.235-239
Hauptverfasser: Bielke, W., Blaschke, R.J., Miescher, G.C., Zürcher, G., Andres, A.-C., Ziemiecki, A.
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Sprache:eng
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Zusammenfassung:Using degenerate oligos corresponding to two highly conserved motifs within the protein kinase catalytic domain and a PCR-based cloning strategy, we have isolated a cDNA fragment encoding a new member of the Ser/Thr (serine/threonine) familiy of protein kinases. Expression analysis revealed that the fragment recognized two transcripts (1.6 and 1.4 kb) exclusively in testis. Using this fragment as a probe, we have cloned a full-length cDNA from a mouse testis cDNA library. The sequence has a 1092-bp open reading frame encoding a protein of 364 amino acids. The N-terminally localized kinase catalytic domain has all the conserved motifs found in other Ser/Thr kinases. Northern blot analysis using the full-length sequence as a probe revealed that the cloned gene corresponds to the 1.6-kb transcript, suggesting the existence of at least two testis-specific novel Ser/Thr kinases. We propose the name festis-specific Kinase-1 ( TSK-1) for the gene described here. A GenEMBL databank search revealed highest homology to the human gene encoding rac protein kinase-β and the group of yeast Ser/Thr kinases encoded by SNF-1, nim-1, KIN-1 and KIN-2.
ISSN:0378-1119
1879-0038
DOI:10.1016/0378-1119(94)90762-5