Abstract:
:The carboxy-terminal half of the c-src protein fused to the protein A moiety was expressed in bacteria. The protein A/truncated c-src fusion protein, which does not have SH2 and SH3 domains, is found in the periplasmic space allowing for a simple one-step purification and demonstrated high efficiency in autophosphorylation and exogeneous substrate phosphorylation. The missense mutation at codon 294 (Ile-->Thr), which is located in the ATP-binding domain of the c-src, resulted in dramatic reduction of tyrosine kinase activity of the fusion protein. Using the fusion protein, we also revealed that staurosporin, a well-known kinase inhibitor, directly affects autophosphorylation of the C-terminal half of the c-src protein. This truncated c-src expression system provides a good source of enzyme for diverse experiments and is an ideal model for understanding the implication of structural alterations in the catalytic activity of the c-src kinase by site-directed mutagenesis experiments.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Saya H,Lee PS,Nishi T,Izawa I,Nakajima M,Gallick GE,Levin VAdoi
10.1016/0014-5793(93)80174-ssubject
Has Abstractpub_date
1993-07-26 00:00:00pages
224-30issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(93)80174-Sjournal_volume
327pub_type
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