Naslov
CHARACTERIZATION OF BRUTON’S TYROSINE KINASE GENE AND PROTEIN FROM MARINE SPONGE SUBERITES DOMUNCULA

Autori
Perina, Dragutin ; Mikoč ; Andreja, Imešek, Mirna ; Harcet, Matija ; Sladojević, Dujo ; Ćetković, Helena

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Book of Abstracts of the 10th Congress of the Croatian Society of Biochemistry and Molecular Biology with the international participation "The secret life of biomolecules", HDBMB 2010 / Kovarik, Zrinka ; Varljen, Jadranka - Rijeka : Hrvatsko Društvo za Biotehnologiju, 2010

Skup
Biochemistry and Molecular Biology with international participation "The secret life of biomolecules", HDBMB 2010

Mjesto i datum
Opatija, Hrvatska, 15.09.2010. - 18.09.2010

Vrsta sudjelovanja
Poster

Vrsta recenzije
Domaća recenzija

Ključne riječi
Porifera; Btk; Tec family PTK; gene structure

Sažetak
Bruton’s tyrosine kinase (Btk) is a member of the Tec family of protein tyrosine kinases (PTKs). This cytoplasmic tyrosine kinase is expressed in B cells and myeloid cells in human. It is crucial for maturation of B- lineage lymphoid cells. Mutations in the gene encoding human Btk result in hereditary immunodeficiency X-linked agammaglobulinemia (XLA). Btk-like 700-aa-long protein from the marine sponge Suberites domuncula (Demospongia) was previously predicted from the nucleotide sequence of one sponge cDNA. Herein we report new evidence on sponge Btk-like gene/protein. Gene coding for sponge Btk-like protein was fully characterized. Position and phase of 16 identified sponge introns were compared with those from homologue genes from other organisms. Phylogenetic analysis revealed that Btk protein is probably most ancient member of Tec family of PTKs and that other members arose from a common gene present in the chordate ancestor. Sponge Btk-like protein probably reflects characteristics of the protein ancestral to Tec family, before the duplications and diversifications within this family. Sponge Btk-like cDNA was therefore cloned and overexpressed using pET15b and E.coli as host. Kinase activity of purified protein was compared to human Btk activity. Our results indicate that this ancestral-type protein was structurally and functionally similar to the highly sophisticated multifunctional enzyme it is today of which functions are usually associated with higher Metazoans.

Izvorni jezik
Engleski

Znanstvena područja
Biologija

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