tailieunhanh - Báo cáo khoa học: Purification and structural study of the b form of human cAMP-dependent protein kinase inhibitor

Thebform of human cAMP-dependent protein kinase inhibitor (human PKIb), a novel heat-stable protein, was isolated with high yield using a bacterial expression system. Assays of PKI activity demonstrated that purified PKIb inhibits the catalytic subunit of cAMP-dependent protein kinase. FTIR, Raman spectroscopy and CD experiments implied that human PKIbcontained only small amounts of a-helix andb-structures, but large amounts of random coil and turn structures, which may explain its high thermosta-bility. The details of its conformational changes in response to heat were studied by CD experiments for the first time, revealing that the protein unfolded at high temperature and refolded when decreased to room temperature | Eur. J. Biochem. 271 1768-1773 2004 FEBS 2004 doi Purification and structural study of the b form of human cAMP-dependent protein kinase inhibitor Rong Jin1 Linsen Dai1 Jinbiao Zheng1 and Chaoneng Ji2 1Center of Analysis and Measurement and 2State Key Laboratory of Genetic Engineering School of Life Sciences Fudan University Shanghai PR Chína The b form of human cAMP-dependent protein kinase inhibitor human PKIb a novel heat-stable protein was isolated with high yield using a bacterial expression system. Assays of PKI activity demonstrated that purified PKIb inhibits the catalytic subunit of cAMP-dependent protein kinase. FTIR Raman spectroscopy and CD experiments implied that human PKIb contained only small amounts of a-helix and b-structures but large amounts of random coil and turn structures which may explain its high thermostability. The details of its conformational changes in response to heat were studied by CD experiments for the first time revealing that the protein unfolded at high temperature and refolded when decreased to room temperature. Keywords CD FTIR human PKIb MS Raman spectroscopy. Signaling through cAMP-dependent protein kinase cAPK is a common pathway for many cellular processes. Regulation of cAPK is achieved by both inhibition and subcellular localization. The best understood control mechanism for cAPK activity is achieved through the regulatory R subunit. Two catalytic C subunits bind to a dimer of R subunits to yield an inactive holoenzyme. Cooperative binding of two molecules of cAMP to each R subunit causes dissociation of the holoenzyme complex and release of two active C subunits 1 2 . In addition there is a second level of regulation of cAPK activity by protein kinase inhibitors PKIs . The PKIs are specific and potent inhibitors of the C subunit however unlike the R subunit PKI inhibition of the C subunit is not relieved by cAMP 3-5 . Moreover the PKIs also serve to localize the C subunit in the cell.

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