| Autor: |
Dechert, Ute, Weber, Peter, König, Bernd, Ortwein, Claus, Nilson, Iris, Linxweiler, Winfried, Wollny, Eric, Gassen, Hans G. |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 11/1/94, Vol. 225 Issue 3, p45-49, 5p |
| Abstrakt: |
To further characterize a protein kinase present in porcine brain microvessels, a eDNA library using porcine microvessel poly(A) RNA was screened with polyclonal antibodies raised against the native protein kinase. Since no full-length eDNA clone could be obtained, the missing sequence information was completed using two subsequent polymerase chain reactions. The amplified tran- scripts were cloned and the sequence determined. Additionally, a genomic DNA library from porcine kidney was screened to substantiate the results obtained from the polymerase chain reaction. Earlier hints of a relation to a subclass of the family of heat-shock proteins (HSPs) based upon a close sequence similarity at its amino-terminus could be confirmed by comparison of the full-length eDNA sequences. Common protein kinase congensus sequences, a targeting sequence for proteins of the endoplasmic reticulum at the carboxy-terminus as well as a hydrophobic leader sequence in the amino-terminal region of the protein could also be identified. Furthermore, a set of membrane- associated substrate proteins of this enzyme could be detected in brain capillaries. The results indicate that at least some members of the HSP 90 subfamily undergo autophosphorylation and show protein kinase activity by phosphorylating substrate proteins in vitro. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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